Mercury in PDB 1piz: Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Enzymatic activity of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
All present enzymatic activity of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH:
1.17.4.1;
Protein crystallography data
The structure of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH, PDB code: 1piz
was solved by
W.C.Voegtli,
M.Sommerhalter,
L.Saleh,
J.Baldwin,
J.M.Bollinger Jr.,
A.C.Rosenzweig,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
23.85 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
74.000,
84.200,
114.200,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.7 /
24.2
|
Other elements in 1piz:
The structure of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH also contains other interesting chemical elements:
Mercury Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
11;
Binding sites:
The binding sites of Mercury atom in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
(pdb code 1piz). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 11 binding sites of Mercury where determined in the
Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH, PDB code: 1piz:
Jump to Mercury binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Mercury binding site 1 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 1 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg378
b:20.5
occ:1.00
|
SG
|
A:CYS272
|
2.4
|
14.4
|
1.0
|
OH
|
A:TYR194
|
2.8
|
15.3
|
1.0
|
CB
|
A:CYS272
|
3.2
|
14.2
|
1.0
|
O
|
A:ALA265
|
3.5
|
22.2
|
1.0
|
CZ
|
A:TYR194
|
3.8
|
15.5
|
1.0
|
CA
|
A:LYS269
|
3.8
|
21.6
|
1.0
|
CE2
|
A:TYR194
|
3.8
|
15.4
|
1.0
|
CE
|
A:MET198
|
4.0
|
14.2
|
1.0
|
CD2
|
A:LEU321
|
4.1
|
12.7
|
1.0
|
CB
|
A:LYS269
|
4.1
|
22.8
|
1.0
|
C
|
A:ALA265
|
4.4
|
22.0
|
1.0
|
N
|
A:LYS269
|
4.4
|
22.5
|
1.0
|
O
|
A:HOH410
|
4.5
|
21.0
|
1.0
|
O
|
A:CYS268
|
4.7
|
22.9
|
1.0
|
O
|
A:LYS269
|
4.7
|
18.6
|
1.0
|
CA
|
A:ALA265
|
4.7
|
20.8
|
1.0
|
CA
|
A:CYS272
|
4.7
|
14.0
|
1.0
|
C
|
A:LYS269
|
4.7
|
20.1
|
1.0
|
C
|
A:CYS268
|
4.8
|
24.1
|
1.0
|
CB
|
A:ALA265
|
4.8
|
20.4
|
1.0
|
CG
|
A:LEU321
|
4.9
|
12.9
|
1.0
|
CG
|
A:MET198
|
5.0
|
14.1
|
1.0
|
|
Mercury binding site 2 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 2 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg379
b:19.0
occ:1.00
|
SG
|
A:CYS196
|
2.3
|
15.7
|
1.0
|
O
|
A:CYS196
|
3.1
|
12.6
|
1.0
|
CB
|
A:CYS196
|
3.3
|
13.6
|
1.0
|
CA
|
A:CYS196
|
3.4
|
12.2
|
1.0
|
CD1
|
A:TYR157
|
3.5
|
12.1
|
1.0
|
CE1
|
A:TYR157
|
3.5
|
12.9
|
1.0
|
C
|
A:CYS196
|
3.6
|
12.2
|
1.0
|
CG
|
A:TYR157
|
3.9
|
13.0
|
1.0
|
CZ
|
A:TYR157
|
3.9
|
12.9
|
1.0
|
CB
|
A:TYR156
|
4.1
|
23.6
|
1.0
|
CD2
|
A:TYR157
|
4.2
|
12.6
|
1.0
|
CE2
|
A:TYR157
|
4.2
|
12.5
|
1.0
|
CB
|
A:SER199
|
4.2
|
11.2
|
1.0
|
N
|
A:TYR157
|
4.2
|
17.1
|
1.0
|
CD1
|
A:TYR156
|
4.2
|
28.8
|
1.0
|
CG
|
A:TYR156
|
4.4
|
27.2
|
1.0
|
CA
|
A:TYR157
|
4.5
|
15.2
|
1.0
|
C
|
A:TYR156
|
4.6
|
18.8
|
1.0
|
OH
|
A:TYR157
|
4.6
|
13.4
|
1.0
|
N
|
A:VAL200
|
4.7
|
9.7
|
1.0
|
O
|
A:ILE153
|
4.7
|
15.7
|
1.0
|
CB
|
A:TYR157
|
4.7
|
14.5
|
1.0
|
N
|
A:LEU197
|
4.8
|
11.7
|
1.0
|
N
|
A:CYS196
|
4.8
|
11.3
|
1.0
|
OG
|
A:SER199
|
4.8
|
12.2
|
1.0
|
CB
|
A:VAL200
|
5.0
|
11.2
|
1.0
|
|
Mercury binding site 3 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 3 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg380
b:28.9
occ:1.00
|
SG
|
A:CYS214
|
2.3
|
19.4
|
1.0
|
O
|
A:VAL210
|
2.8
|
14.1
|
1.0
|
N
|
A:CYS214
|
3.3
|
15.2
|
1.0
|
CB
|
A:CYS214
|
3.5
|
18.0
|
1.0
|
CA
|
A:CYS214
|
3.6
|
16.3
|
1.0
|
CB
|
A:ALA213
|
3.8
|
14.3
|
1.0
|
CD1
|
A:LEU299
|
3.9
|
19.3
|
1.0
|
C
|
A:VAL210
|
4.0
|
14.7
|
1.0
|
C
|
A:ALA213
|
4.0
|
14.6
|
1.0
|
CG1
|
A:VAL210
|
4.0
|
15.8
|
1.0
|
CD1
|
A:LEU304
|
4.2
|
18.5
|
1.0
|
CA
|
A:ALA213
|
4.4
|
14.6
|
1.0
|
CG
|
A:LEU304
|
4.5
|
17.8
|
1.0
|
O
|
A:HOH459
|
4.5
|
36.0
|
1.0
|
CA
|
A:VAL210
|
4.8
|
14.9
|
1.0
|
O
|
A:ALA213
|
4.8
|
14.3
|
1.0
|
CB
|
A:LEU304
|
4.9
|
17.6
|
1.0
|
N
|
A:ALA213
|
4.9
|
14.8
|
1.0
|
N
|
A:SER211
|
5.0
|
14.1
|
1.0
|
|
Mercury binding site 4 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 4 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 4 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg381
b:29.3
occ:0.50
|
SG
|
A:CYS305
|
2.3
|
25.6
|
1.0
|
CB
|
A:CYS305
|
3.4
|
19.6
|
1.0
|
CD
|
A:GLU309
|
3.4
|
15.7
|
1.0
|
OE2
|
A:GLU309
|
3.5
|
16.7
|
1.0
|
C
|
A:CYS305
|
3.6
|
17.6
|
1.0
|
O
|
A:CYS305
|
3.7
|
17.0
|
1.0
|
OE1
|
A:GLU309
|
3.7
|
16.2
|
1.0
|
N
|
A:GLN306
|
3.7
|
16.8
|
1.0
|
CG
|
A:GLU309
|
3.9
|
15.0
|
1.0
|
CA
|
A:GLN306
|
4.1
|
16.4
|
1.0
|
CA
|
A:CYS305
|
4.1
|
18.4
|
1.0
|
NZ
|
A:LYS284
|
4.4
|
17.9
|
1.0
|
CG
|
A:GLN306
|
4.4
|
18.6
|
1.0
|
CE
|
A:LYS284
|
4.4
|
16.5
|
1.0
|
O
|
A:HOH493
|
4.5
|
21.0
|
1.0
|
NH2
|
A:ARG328
|
4.7
|
35.4
|
1.0
|
CB
|
A:GLN306
|
4.8
|
17.4
|
1.0
|
O
|
A:ASP302
|
4.9
|
20.1
|
1.0
|
|
Mercury binding site 5 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 5 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 5 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg382
b:91.4
occ:0.50
|
SG
|
A:CYS268
|
2.5
|
34.2
|
1.0
|
CB
|
A:CYS268
|
2.7
|
27.8
|
1.0
|
O
|
A:ILE264
|
3.3
|
16.5
|
1.0
|
CG2
|
A:ILE264
|
3.4
|
15.9
|
1.0
|
N
|
A:CYS268
|
3.4
|
26.1
|
1.0
|
CA
|
A:CYS268
|
3.6
|
26.2
|
1.0
|
CD
|
A:LYS191
|
3.7
|
17.7
|
1.0
|
CG
|
A:LYS191
|
3.7
|
16.3
|
1.0
|
CE
|
A:LYS191
|
4.1
|
19.5
|
1.0
|
C
|
A:ILE264
|
4.1
|
17.6
|
1.0
|
CB
|
A:GLU267
|
4.2
|
29.0
|
1.0
|
C
|
A:GLU267
|
4.2
|
26.8
|
1.0
|
CA
|
A:ILE264
|
4.2
|
16.9
|
1.0
|
CB
|
A:LYS191
|
4.2
|
14.1
|
1.0
|
CB
|
A:ILE264
|
4.3
|
16.2
|
1.0
|
NZ
|
A:LYS191
|
4.7
|
20.7
|
1.0
|
OE1
|
A:GLU267
|
4.7
|
34.6
|
1.0
|
CA
|
A:GLU267
|
4.8
|
27.1
|
1.0
|
CG1
|
A:ILE264
|
4.8
|
15.8
|
1.0
|
O
|
A:GLU267
|
4.9
|
26.7
|
1.0
|
C
|
A:CYS268
|
4.9
|
24.1
|
1.0
|
CA
|
A:LYS191
|
4.9
|
12.2
|
1.0
|
|
Mercury binding site 6 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 6 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 6 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg378
b:32.1
occ:1.00
|
CB
|
B:CYS196
|
2.7
|
8.0
|
1.0
|
CA
|
B:CYS196
|
2.8
|
11.3
|
1.0
|
SG
|
B:CYS196
|
3.0
|
2.0
|
1.0
|
O
|
B:CYS196
|
3.2
|
11.3
|
1.0
|
C
|
B:CYS196
|
3.4
|
11.3
|
1.0
|
CG2
|
B:VAL200
|
3.4
|
10.6
|
1.0
|
CB
|
B:TYR156
|
3.5
|
17.2
|
1.0
|
CD1
|
B:TYR157
|
3.5
|
13.5
|
1.0
|
CG
|
B:TYR157
|
3.7
|
12.9
|
1.0
|
CE1
|
B:TYR157
|
3.7
|
12.6
|
1.0
|
CD2
|
B:TYR157
|
3.8
|
12.5
|
1.0
|
N
|
B:TYR157
|
3.8
|
13.8
|
1.0
|
CZ
|
B:TYR157
|
3.9
|
12.7
|
1.0
|
CE2
|
B:TYR157
|
4.0
|
12.2
|
1.0
|
C
|
B:TYR156
|
4.1
|
14.5
|
1.0
|
CA
|
B:TYR157
|
4.2
|
13.0
|
1.0
|
N
|
B:CYS196
|
4.2
|
13.2
|
1.0
|
CB
|
B:SER199
|
4.3
|
12.6
|
1.0
|
CA
|
B:TYR156
|
4.5
|
15.3
|
1.0
|
CB
|
B:TYR157
|
4.5
|
12.7
|
1.0
|
O
|
B:ILE153
|
4.5
|
16.9
|
1.0
|
OG
|
B:SER199
|
4.5
|
14.9
|
1.0
|
N
|
B:VAL200
|
4.6
|
9.6
|
1.0
|
N
|
B:LEU197
|
4.6
|
12.2
|
1.0
|
O
|
B:TYR156
|
4.6
|
13.5
|
1.0
|
CG
|
B:TYR156
|
4.6
|
18.9
|
1.0
|
OH
|
B:TYR157
|
4.7
|
11.1
|
1.0
|
CB
|
B:VAL200
|
4.7
|
10.7
|
1.0
|
O
|
B:LEU195
|
4.9
|
15.5
|
1.0
|
|
Mercury binding site 7 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 7 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 7 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg379
b:15.4
occ:0.50
|
SG
|
B:CYS272
|
2.4
|
24.3
|
1.0
|
SG
|
B:CYS268
|
2.4
|
28.0
|
1.0
|
O
|
B:CYS268
|
2.7
|
31.5
|
1.0
|
CB
|
B:CYS268
|
3.2
|
30.4
|
1.0
|
C
|
B:CYS268
|
3.3
|
31.1
|
1.0
|
CB
|
B:CYS272
|
3.4
|
21.2
|
1.0
|
CD2
|
B:TYR194
|
3.6
|
13.7
|
1.0
|
CA
|
B:CYS268
|
3.9
|
30.9
|
1.0
|
N
|
B:CYS272
|
3.9
|
21.4
|
1.0
|
CD2
|
B:LEU195
|
3.9
|
16.4
|
1.0
|
CE2
|
B:TYR194
|
4.0
|
14.0
|
1.0
|
CA
|
B:CYS272
|
4.1
|
20.7
|
1.0
|
N
|
B:LYS269
|
4.2
|
31.2
|
1.0
|
O
|
B:ALA265
|
4.5
|
25.2
|
1.0
|
CA
|
B:LYS269
|
4.5
|
31.2
|
1.0
|
N
|
B:CYS268
|
4.7
|
30.8
|
1.0
|
CB
|
B:GLU271
|
4.7
|
23.0
|
1.0
|
CG
|
B:TYR194
|
4.8
|
13.5
|
1.0
|
C
|
B:GLU271
|
4.9
|
22.2
|
1.0
|
CA
|
B:ALA265
|
4.9
|
24.8
|
1.0
|
|
Mercury binding site 8 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 8 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 8 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg380
b:33.5
occ:0.50
|
SG
|
B:CYS214
|
2.6
|
8.6
|
1.0
|
O
|
B:VAL210
|
2.8
|
16.4
|
1.0
|
CD1
|
B:LEU304
|
2.9
|
28.9
|
1.0
|
N
|
B:CYS214
|
3.2
|
17.4
|
1.0
|
CG
|
B:LEU304
|
3.4
|
28.2
|
1.0
|
CB
|
B:CYS214
|
3.5
|
15.4
|
1.0
|
CA
|
B:CYS214
|
3.6
|
16.5
|
1.0
|
CB
|
B:ALA213
|
3.7
|
17.4
|
1.0
|
C
|
B:VAL210
|
3.9
|
16.8
|
1.0
|
CG1
|
B:VAL210
|
3.9
|
19.1
|
1.0
|
C
|
B:ALA213
|
4.0
|
17.1
|
1.0
|
CB
|
B:LEU304
|
4.1
|
26.7
|
1.0
|
CD1
|
B:LEU299
|
4.2
|
39.7
|
1.0
|
CA
|
B:ALA213
|
4.4
|
16.9
|
1.0
|
CD2
|
B:LEU299
|
4.4
|
39.7
|
1.0
|
CA
|
B:VAL210
|
4.6
|
17.0
|
1.0
|
CD2
|
B:LEU304
|
4.6
|
28.8
|
1.0
|
N
|
B:ALA213
|
4.7
|
16.6
|
1.0
|
O
|
B:ALA213
|
4.8
|
17.1
|
1.0
|
CG
|
B:LEU299
|
4.8
|
39.1
|
1.0
|
CA
|
B:LEU304
|
4.9
|
25.9
|
1.0
|
N
|
B:SER211
|
4.9
|
16.3
|
1.0
|
CB
|
B:VAL210
|
4.9
|
17.7
|
1.0
|
|
Mercury binding site 9 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 9 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 9 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg381
b:67.9
occ:0.50
|
O
|
B:CYS272
|
2.6
|
18.6
|
1.0
|
CA
|
B:CYS272
|
2.9
|
20.7
|
1.0
|
CB
|
B:CYS272
|
2.9
|
21.2
|
1.0
|
C
|
B:CYS272
|
3.1
|
19.4
|
1.0
|
CG
|
B:MET198
|
3.2
|
18.0
|
1.0
|
CB
|
B:MET198
|
3.2
|
15.0
|
1.0
|
SG
|
B:CYS272
|
3.3
|
24.3
|
1.0
|
SD
|
B:MET198
|
3.5
|
19.9
|
1.0
|
CB
|
B:LEU275
|
3.5
|
21.5
|
1.0
|
CD1
|
B:LEU275
|
3.6
|
23.6
|
1.0
|
CD2
|
B:LEU275
|
3.6
|
23.6
|
1.0
|
CG
|
B:LEU275
|
3.8
|
22.9
|
1.0
|
CD2
|
B:PHE276
|
4.0
|
20.5
|
1.0
|
N
|
B:PHE276
|
4.2
|
19.9
|
1.0
|
N
|
B:CYS272
|
4.3
|
21.4
|
1.0
|
N
|
B:TYR273
|
4.3
|
18.6
|
1.0
|
CA
|
B:MET198
|
4.5
|
12.7
|
1.0
|
CA
|
B:LEU275
|
4.6
|
20.1
|
1.0
|
CD1
|
B:LEU321
|
4.6
|
21.6
|
1.0
|
C
|
B:MET198
|
4.6
|
11.6
|
1.0
|
C
|
B:LEU275
|
4.7
|
20.1
|
1.0
|
CE2
|
B:PHE276
|
4.7
|
19.9
|
1.0
|
CB
|
B:PHE276
|
4.7
|
19.9
|
1.0
|
CG
|
B:PHE276
|
4.8
|
19.5
|
1.0
|
O
|
B:GLU271
|
4.8
|
21.8
|
1.0
|
O
|
B:MET198
|
4.8
|
11.1
|
1.0
|
N
|
B:LEU275
|
4.9
|
19.7
|
1.0
|
CE
|
B:MET198
|
4.9
|
20.3
|
1.0
|
CA
|
B:PHE276
|
4.9
|
19.1
|
1.0
|
C
|
B:GLU271
|
5.0
|
22.2
|
1.0
|
|
Mercury binding site 10 out
of 11 in 1piz
Go back to
Mercury Binding Sites List in 1piz
Mercury binding site 10 out
of 11 in the Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 10 of Ribonucleotide Reductase R2 D84E Mutant Soaked with Ferrous Ions at Neutral pH within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg382
b:44.4
occ:0.50
|
CE
|
B:LYS284
|
2.4
|
27.3
|
1.0
|
SG
|
B:CYS305
|
2.5
|
28.5
|
1.0
|
NZ
|
B:LYS284
|
2.6
|
28.4
|
1.0
|
CD
|
B:LYS284
|
2.7
|
27.4
|
1.0
|
CG
|
B:LYS284
|
2.9
|
26.9
|
1.0
|
O
|
B:CYS305
|
3.0
|
22.1
|
1.0
|
HG
|
B:HG383
|
3.5
|
56.8
|
0.5
|
CG
|
B:GLU309
|
3.5
|
19.8
|
1.0
|
C
|
B:CYS305
|
3.6
|
22.9
|
1.0
|
CA
|
B:CYS305
|
3.6
|
23.8
|
1.0
|
CB
|
B:CYS305
|
3.6
|
24.7
|
1.0
|
OE2
|
B:GLU309
|
3.9
|
22.1
|
1.0
|
CB
|
B:LYS284
|
4.0
|
26.1
|
1.0
|
CD
|
B:GLU309
|
4.0
|
21.7
|
1.0
|
CB
|
B:VAL308
|
4.4
|
15.3
|
1.0
|
CG1
|
B:VAL308
|
4.6
|
15.1
|
1.0
|
N
|
B:GLU309
|
4.7
|
16.4
|
1.0
|
N
|
B:GLN306
|
4.7
|
21.2
|
1.0
|
CB
|
B:GLU309
|
4.8
|
18.1
|
1.0
|
N
|
B:CYS305
|
5.0
|
24.6
|
1.0
|
|
Reference:
W.C.Voegtli,
M.Sommerhalter,
L.Saleh,
J.Baldwin,
J.M.Bollinger Jr.,
A.C.Rosenzweig.
Variable Coordination Geometries at the Diiron(II) Active Site of Ribonucleotide Reductase R2. J.Am.Chem.Soc. V. 125 15822 2003.
ISSN: ISSN 0002-7863
PubMed: 14677973
DOI: 10.1021/JA0370387
Page generated: Sun Aug 11 01:02:47 2024
|