Mercury in PDB 1rnr: Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Enzymatic activity of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
All present enzymatic activity of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein:
1.17.4.1;
Protein crystallography data
The structure of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein, PDB code: 1rnr
was solved by
A.Aberg,
P.Nordlund,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
10.00 /
2.50
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.100,
85.300,
115.700,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.6 /
n/a
|
Other elements in 1rnr:
The structure of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein also contains other interesting chemical elements:
Mercury Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
14;
Binding sites:
The binding sites of Mercury atom in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
(pdb code 1rnr). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 14 binding sites of Mercury where determined in the
Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein, PDB code: 1rnr:
Jump to Mercury binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Mercury binding site 1 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 1 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg403
b:26.4
occ:1.00
|
SG
|
A:CYS196
|
2.0
|
13.9
|
1.0
|
O
|
A:HOH417
|
3.0
|
36.1
|
1.0
|
HG
|
A:HG406
|
3.1
|
10.6
|
0.1
|
O
|
A:CYS196
|
3.3
|
14.1
|
1.0
|
CB
|
A:CYS196
|
3.3
|
15.5
|
1.0
|
CA
|
A:CYS196
|
3.4
|
14.4
|
1.0
|
CE1
|
A:TYR157
|
3.5
|
12.1
|
1.0
|
CD1
|
A:TYR157
|
3.5
|
14.3
|
1.0
|
C
|
A:CYS196
|
3.6
|
14.0
|
1.0
|
CB
|
A:TYR156
|
3.7
|
35.1
|
1.0
|
CZ
|
A:TYR157
|
3.7
|
15.1
|
1.0
|
CG
|
A:TYR157
|
3.8
|
15.2
|
1.0
|
CG2
|
A:VAL200
|
3.9
|
13.3
|
1.0
|
CE2
|
A:TYR157
|
3.9
|
13.2
|
1.0
|
CD2
|
A:TYR157
|
4.0
|
14.5
|
1.0
|
N
|
A:TYR157
|
4.2
|
21.1
|
1.0
|
CB
|
A:SER199
|
4.3
|
15.7
|
1.0
|
OH
|
A:TYR157
|
4.4
|
18.1
|
1.0
|
CG
|
A:TYR156
|
4.4
|
41.7
|
1.0
|
C
|
A:TYR156
|
4.6
|
25.2
|
1.0
|
CA
|
A:TYR157
|
4.6
|
20.4
|
1.0
|
N
|
A:VAL200
|
4.7
|
14.8
|
1.0
|
N
|
A:LEU197
|
4.7
|
12.4
|
1.0
|
CB
|
A:TYR157
|
4.8
|
16.8
|
1.0
|
CD1
|
A:TYR156
|
4.8
|
45.6
|
1.0
|
CA
|
A:TYR156
|
4.8
|
28.9
|
1.0
|
N
|
A:CYS196
|
4.8
|
14.2
|
1.0
|
O
|
A:ILE153
|
4.8
|
35.0
|
1.0
|
OG
|
A:SER199
|
4.9
|
20.3
|
1.0
|
|
Mercury binding site 2 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 2 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg404
b:27.2
occ:1.00
|
HG
|
A:HG407
|
1.8
|
42.0
|
0.3
|
SG
|
A:CYS272
|
2.2
|
42.2
|
1.0
|
OH
|
A:TYR194
|
3.0
|
16.3
|
1.0
|
CB
|
A:CYS272
|
3.3
|
29.3
|
1.0
|
O
|
A:ALA265
|
3.7
|
21.6
|
1.0
|
CA
|
A:LYS269
|
3.7
|
24.4
|
1.0
|
CE
|
A:MET198
|
3.8
|
5.8
|
1.0
|
CE2
|
A:TYR194
|
3.9
|
13.0
|
1.0
|
CZ
|
A:TYR194
|
3.9
|
15.3
|
1.0
|
CD2
|
A:LEU321
|
3.9
|
9.2
|
1.0
|
CB
|
A:LYS269
|
4.3
|
25.8
|
1.0
|
N
|
A:LYS269
|
4.3
|
21.6
|
1.0
|
CG
|
A:LYS269
|
4.4
|
31.3
|
1.0
|
C
|
A:ALA265
|
4.5
|
21.6
|
1.0
|
O
|
A:LYS269
|
4.5
|
24.8
|
1.0
|
O
|
A:HOH429
|
4.5
|
8.0
|
1.0
|
CA
|
A:ALA265
|
4.6
|
19.9
|
1.0
|
C
|
A:LYS269
|
4.7
|
24.6
|
1.0
|
CB
|
A:ALA265
|
4.7
|
16.9
|
1.0
|
C
|
A:CYS268
|
4.8
|
22.8
|
1.0
|
CA
|
A:CYS272
|
4.8
|
26.4
|
1.0
|
O
|
A:CYS268
|
4.8
|
21.9
|
1.0
|
CG
|
A:LEU321
|
4.8
|
11.1
|
1.0
|
CG
|
A:MET198
|
5.0
|
12.4
|
1.0
|
|
Mercury binding site 3 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 3 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg405
b:28.8
occ:0.75
|
SG
|
A:CYS214
|
2.0
|
22.4
|
1.0
|
O
|
A:HOH414
|
2.3
|
25.8
|
1.0
|
O
|
A:VAL210
|
3.0
|
24.0
|
1.0
|
N
|
A:CYS214
|
3.1
|
24.3
|
1.0
|
CB
|
A:CYS214
|
3.2
|
24.4
|
1.0
|
CA
|
A:CYS214
|
3.5
|
24.5
|
1.0
|
CB
|
A:ALA213
|
3.7
|
26.2
|
1.0
|
CD1
|
A:LEU304
|
3.8
|
26.0
|
1.0
|
C
|
A:ALA213
|
3.9
|
23.8
|
1.0
|
C
|
A:VAL210
|
3.9
|
22.9
|
1.0
|
CG1
|
A:VAL210
|
4.0
|
15.4
|
1.0
|
CG
|
A:LEU304
|
4.2
|
26.1
|
1.0
|
CD1
|
A:LEU299
|
4.3
|
26.6
|
1.0
|
CA
|
A:ALA213
|
4.4
|
25.5
|
1.0
|
CA
|
A:VAL210
|
4.5
|
20.2
|
1.0
|
O
|
A:ALA213
|
4.6
|
22.5
|
1.0
|
CD2
|
A:LEU299
|
4.7
|
26.5
|
1.0
|
CB
|
A:LEU304
|
4.8
|
23.5
|
1.0
|
N
|
A:ALA213
|
4.8
|
27.6
|
1.0
|
O
|
A:HOH419
|
4.9
|
23.4
|
1.0
|
CG
|
A:LEU299
|
4.9
|
27.2
|
1.0
|
N
|
A:SER211
|
4.9
|
24.1
|
1.0
|
CB
|
A:VAL210
|
4.9
|
16.8
|
1.0
|
|
Mercury binding site 4 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 4 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 4 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg406
b:10.6
occ:0.10
|
SG
|
A:CYS196
|
1.8
|
13.9
|
1.0
|
CB
|
A:CYS196
|
3.0
|
15.5
|
1.0
|
HG
|
A:HG403
|
3.1
|
26.4
|
1.0
|
CE1
|
A:TYR157
|
3.1
|
12.1
|
1.0
|
CD1
|
A:LEU95
|
3.5
|
12.6
|
1.0
|
CG2
|
A:VAL200
|
3.5
|
13.3
|
1.0
|
C
|
A:CYS196
|
3.5
|
14.0
|
1.0
|
CD1
|
A:TYR157
|
3.7
|
14.3
|
1.0
|
O
|
A:CYS196
|
3.8
|
14.1
|
1.0
|
N
|
A:LEU197
|
3.8
|
12.4
|
1.0
|
CA
|
A:CYS196
|
3.8
|
14.4
|
1.0
|
CZ
|
A:TYR157
|
3.9
|
15.1
|
1.0
|
OH
|
A:TYR157
|
4.1
|
18.1
|
1.0
|
CA
|
A:LEU197
|
4.4
|
14.4
|
1.0
|
CD2
|
A:LEU95
|
4.5
|
11.8
|
1.0
|
CD2
|
A:LEU197
|
4.5
|
12.2
|
1.0
|
CG
|
A:LEU95
|
4.5
|
14.0
|
1.0
|
CD2
|
A:LEU160
|
4.6
|
11.5
|
1.0
|
CB
|
A:VAL200
|
4.7
|
14.3
|
1.0
|
CG
|
A:TYR157
|
4.9
|
15.2
|
1.0
|
CG
|
A:LEU197
|
5.0
|
15.3
|
1.0
|
CE2
|
A:TYR157
|
5.0
|
13.2
|
1.0
|
O
|
A:LEU193
|
5.0
|
11.6
|
1.0
|
|
Mercury binding site 5 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 5 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 5 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg407
b:42.0
occ:0.30
|
SG
|
A:CYS272
|
1.7
|
42.2
|
1.0
|
HG
|
A:HG404
|
1.8
|
27.2
|
1.0
|
CB
|
A:CYS272
|
1.8
|
29.3
|
1.0
|
CE2
|
A:TYR194
|
3.3
|
13.0
|
1.0
|
CA
|
A:CYS272
|
3.3
|
26.4
|
1.0
|
OH
|
A:TYR194
|
3.5
|
16.3
|
1.0
|
O
|
A:CYS268
|
3.7
|
21.9
|
1.0
|
CA
|
A:LYS269
|
3.8
|
24.4
|
1.0
|
N
|
A:CYS272
|
3.8
|
24.3
|
1.0
|
CE
|
A:MET198
|
3.8
|
5.8
|
1.0
|
CZ
|
A:TYR194
|
3.9
|
15.3
|
1.0
|
C
|
A:CYS268
|
4.0
|
22.8
|
1.0
|
CG
|
A:MET198
|
4.1
|
12.4
|
1.0
|
O
|
A:LYS269
|
4.1
|
24.8
|
1.0
|
N
|
A:LYS269
|
4.1
|
21.6
|
1.0
|
C
|
A:LYS269
|
4.3
|
24.6
|
1.0
|
C
|
A:CYS272
|
4.3
|
24.6
|
1.0
|
O
|
A:ALA265
|
4.4
|
21.6
|
1.0
|
CD2
|
A:TYR194
|
4.4
|
17.1
|
1.0
|
CD2
|
A:LEU321
|
4.5
|
9.2
|
1.0
|
SD
|
A:MET198
|
4.6
|
12.4
|
1.0
|
CD2
|
A:LEU195
|
4.7
|
20.6
|
1.0
|
CB
|
A:LYS269
|
4.8
|
25.8
|
1.0
|
N
|
A:TYR273
|
4.9
|
22.6
|
1.0
|
|
Mercury binding site 6 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 6 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 6 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg408
b:26.7
occ:0.30
|
OE1
|
A:GLU309
|
3.3
|
30.9
|
1.0
|
CB
|
A:CYS305
|
3.4
|
30.4
|
1.0
|
O
|
A:HOH468
|
3.4
|
50.1
|
1.0
|
C
|
A:CYS305
|
3.6
|
23.5
|
1.0
|
N
|
A:GLN306
|
3.6
|
22.0
|
1.0
|
CD
|
A:GLU309
|
3.7
|
32.0
|
1.0
|
O
|
A:CYS305
|
3.8
|
23.9
|
1.0
|
NZ
|
A:LYS284
|
3.8
|
6.9
|
1.0
|
OE2
|
A:GLU309
|
3.9
|
36.4
|
1.0
|
CA
|
A:GLN306
|
3.9
|
23.1
|
1.0
|
CA
|
A:CYS305
|
4.1
|
25.6
|
1.0
|
CB
|
A:GLN306
|
4.2
|
26.1
|
1.0
|
CE
|
A:LYS284
|
4.5
|
10.7
|
1.0
|
CB
|
A:GLU309
|
4.7
|
25.2
|
1.0
|
CG
|
A:GLU309
|
4.7
|
28.9
|
1.0
|
NH2
|
A:ARG328
|
4.8
|
51.5
|
1.0
|
SG
|
A:CYS305
|
4.8
|
46.5
|
1.0
|
O
|
A:ASP302
|
4.9
|
31.1
|
1.0
|
|
Mercury binding site 7 out
of 14 in 1rnr
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Mercury Binding Sites List in 1rnr
Mercury binding site 7 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 7 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg403
b:32.2
occ:1.00
|
SG
|
B:CYS196
|
2.0
|
11.7
|
1.0
|
O
|
B:HOH421
|
2.3
|
9.7
|
1.0
|
HG
|
B:HG408
|
2.6
|
36.2
|
0.3
|
O
|
B:CYS196
|
3.1
|
13.3
|
1.0
|
CB
|
B:TYR156
|
3.4
|
30.3
|
1.0
|
CA
|
B:CYS196
|
3.4
|
15.7
|
1.0
|
CB
|
B:CYS196
|
3.5
|
14.7
|
1.0
|
C
|
B:CYS196
|
3.5
|
14.1
|
1.0
|
CD1
|
B:TYR157
|
3.7
|
11.9
|
1.0
|
CE1
|
B:TYR157
|
3.7
|
12.6
|
1.0
|
CG2
|
B:VAL200
|
3.8
|
22.2
|
1.0
|
CG
|
B:TYR157
|
3.8
|
11.7
|
1.0
|
CZ
|
B:TYR157
|
3.9
|
11.8
|
1.0
|
N
|
B:TYR157
|
3.9
|
19.5
|
1.0
|
O
|
B:HOH412
|
3.9
|
34.4
|
1.0
|
CD2
|
B:TYR157
|
4.0
|
10.3
|
1.0
|
CE2
|
B:TYR157
|
4.0
|
10.9
|
1.0
|
C
|
B:TYR156
|
4.2
|
23.7
|
1.0
|
CB
|
B:SER199
|
4.3
|
19.1
|
1.0
|
CA
|
B:TYR157
|
4.4
|
17.2
|
1.0
|
CA
|
B:TYR156
|
4.5
|
25.7
|
1.0
|
CG
|
B:TYR156
|
4.5
|
34.0
|
1.0
|
OH
|
B:TYR157
|
4.6
|
10.2
|
1.0
|
O
|
B:ILE153
|
4.6
|
29.4
|
1.0
|
CB
|
B:TYR157
|
4.6
|
15.0
|
1.0
|
N
|
B:VAL200
|
4.6
|
18.4
|
1.0
|
N
|
B:LEU197
|
4.7
|
14.2
|
1.0
|
O
|
B:TYR156
|
4.8
|
24.9
|
1.0
|
N
|
B:CYS196
|
4.8
|
17.9
|
1.0
|
|
Mercury binding site 8 out
of 14 in 1rnr
Go back to
Mercury Binding Sites List in 1rnr
Mercury binding site 8 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 8 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg404
b:46.6
occ:0.40
|
CD1
|
B:LEU304
|
2.3
|
28.9
|
1.0
|
HG
|
B:HG407
|
2.7
|
30.9
|
0.3
|
CD2
|
B:LEU304
|
2.8
|
31.1
|
1.0
|
O
|
B:VAL210
|
2.8
|
26.5
|
1.0
|
SG
|
B:CYS214
|
3.0
|
38.8
|
1.0
|
CG
|
B:LEU304
|
3.1
|
30.2
|
1.0
|
CG1
|
B:VAL210
|
3.5
|
26.6
|
1.0
|
CB
|
B:ALA213
|
3.6
|
21.2
|
1.0
|
N
|
B:CYS214
|
3.7
|
22.6
|
1.0
|
C
|
B:VAL210
|
3.9
|
25.1
|
1.0
|
CD2
|
B:LEU299
|
3.9
|
33.2
|
1.0
|
CB
|
B:CYS214
|
4.2
|
28.0
|
1.0
|
C
|
B:ALA213
|
4.3
|
21.0
|
1.0
|
CA
|
B:VAL210
|
4.3
|
26.4
|
1.0
|
CA
|
B:CYS214
|
4.3
|
23.3
|
1.0
|
CD1
|
B:LEU299
|
4.4
|
34.5
|
1.0
|
CB
|
B:LEU304
|
4.4
|
29.5
|
1.0
|
CA
|
B:ALA213
|
4.5
|
20.9
|
1.0
|
CG
|
B:LEU299
|
4.6
|
34.0
|
1.0
|
CB
|
B:VAL210
|
4.6
|
26.6
|
1.0
|
N
|
B:SER211
|
4.9
|
25.8
|
1.0
|
|
Mercury binding site 9 out
of 14 in 1rnr
Go back to
Mercury Binding Sites List in 1rnr
Mercury binding site 9 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 9 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg405
b:31.5
occ:0.40
|
O
|
B:HOH413
|
1.9
|
45.1
|
1.0
|
SG
|
B:CYS272
|
3.2
|
55.6
|
1.0
|
CE
|
B:MET198
|
3.3
|
25.1
|
1.0
|
OH
|
B:TYR194
|
3.4
|
24.1
|
1.0
|
CE2
|
B:TYR194
|
3.7
|
23.6
|
1.0
|
HG
|
B:HG409
|
3.7
|
56.4
|
0.1
|
CD2
|
B:LEU321
|
3.7
|
34.1
|
1.0
|
O
|
B:ALA265
|
3.8
|
39.4
|
1.0
|
CB
|
B:CYS272
|
4.0
|
45.8
|
1.0
|
CZ
|
B:TYR194
|
4.0
|
23.4
|
1.0
|
CA
|
B:LYS269
|
4.2
|
42.7
|
1.0
|
C
|
B:ALA265
|
4.3
|
39.7
|
1.0
|
CA
|
B:ALA265
|
4.4
|
38.0
|
1.0
|
CB
|
B:ALA265
|
4.5
|
37.5
|
1.0
|
N
|
B:LYS269
|
4.5
|
42.8
|
1.0
|
CG
|
B:LYS269
|
4.5
|
46.2
|
1.0
|
CG
|
B:LEU321
|
4.7
|
35.2
|
1.0
|
C
|
B:CYS268
|
4.8
|
44.1
|
1.0
|
CD2
|
B:TYR194
|
4.8
|
20.9
|
1.0
|
CB
|
B:LYS269
|
4.9
|
42.7
|
1.0
|
CD1
|
B:LEU321
|
5.0
|
34.0
|
1.0
|
|
Mercury binding site 10 out
of 14 in 1rnr
Go back to
Mercury Binding Sites List in 1rnr
Mercury binding site 10 out
of 14 in the Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 10 of Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg406
b:36.0
occ:0.40
|
CG
|
B:MET198
|
2.8
|
25.7
|
1.0
|
O
|
B:CYS272
|
3.0
|
41.3
|
1.0
|
CA
|
B:CYS272
|
3.0
|
43.4
|
1.0
|
CB
|
B:CYS272
|
3.2
|
45.8
|
1.0
|
C
|
B:CYS272
|
3.4
|
40.5
|
1.0
|
SG
|
B:CYS272
|
3.5
|
55.6
|
1.0
|
CD2
|
B:PHE276
|
3.6
|
28.4
|
1.0
|
CB
|
B:MET198
|
3.7
|
22.2
|
1.0
|
CB
|
B:LEU275
|
3.8
|
38.1
|
1.0
|
CD2
|
B:LEU275
|
3.9
|
42.9
|
1.0
|
CE2
|
B:PHE276
|
3.9
|
28.4
|
1.0
|
SD
|
B:MET198
|
4.2
|
27.4
|
1.0
|
N
|
B:CYS272
|
4.2
|
43.4
|
1.0
|
N
|
B:PHE276
|
4.3
|
32.9
|
1.0
|
CG
|
B:LEU275
|
4.4
|
42.2
|
1.0
|
O
|
B:GLU271
|
4.5
|
45.2
|
1.0
|
C
|
B:MET198
|
4.6
|
20.1
|
1.0
|
CG
|
B:PHE276
|
4.6
|
26.5
|
1.0
|
O
|
B:MET198
|
4.6
|
19.5
|
1.0
|
N
|
B:TYR273
|
4.7
|
38.0
|
1.0
|
CA
|
B:MET198
|
4.7
|
21.0
|
1.0
|
CA
|
B:LEU275
|
4.7
|
36.3
|
1.0
|
CE
|
B:MET198
|
4.7
|
25.1
|
1.0
|
C
|
B:LEU275
|
4.8
|
34.6
|
1.0
|
C
|
B:GLU271
|
4.8
|
43.7
|
1.0
|
|
Reference:
A.Aberg,
M.Ormo,
P.Nordlund,
B.M.Sjoberg.
Autocatalytic Generation of Dopa in the Engineered Protein R2 F208Y From Escherichia Coli Ribonucleotide Reductase and Crystal Structure of the Dopa-208 Protein. Biochemistry V. 32 9845 1993.
ISSN: ISSN 0006-2960
PubMed: 8373782
DOI: 10.1021/BI00088A040
Page generated: Sun Aug 11 01:27:06 2024
|