Mercury in PDB 2g87: Crystallographic Model of Bathorhodopsin
Protein crystallography data
The structure of Crystallographic Model of Bathorhodopsin, PDB code: 2g87
was solved by
H.Nakamichi,
T.Okada,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.60
|
Space group
|
P 41
|
Cell size a, b, c (Å), α, β, γ (°)
|
96.490,
96.490,
150.400,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
17.8 /
18.1
|
Other elements in 2g87:
The structure of Crystallographic Model of Bathorhodopsin also contains other interesting chemical elements:
Mercury Binding Sites:
The binding sites of Mercury atom in the Crystallographic Model of Bathorhodopsin
(pdb code 2g87). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 6 binding sites of Mercury where determined in the
Crystallographic Model of Bathorhodopsin, PDB code: 2g87:
Jump to Mercury binding site number:
1;
2;
3;
4;
5;
6;
Mercury binding site 1 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 1 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg901
b:84.4
occ:0.89
|
SG
|
A:CYS264
|
2.7
|
55.4
|
1.0
|
CB
|
A:CYS264
|
3.0
|
50.6
|
1.0
|
OG1
|
A:THR297
|
3.1
|
46.0
|
1.0
|
CD2
|
A:TYR301
|
3.6
|
48.1
|
1.0
|
CA
|
A:CYS264
|
3.7
|
49.3
|
1.0
|
CE2
|
A:TYR301
|
3.9
|
49.3
|
1.0
|
CZ
|
A:PHE294
|
3.9
|
41.5
|
1.0
|
O
|
A:ALA260
|
3.9
|
52.7
|
1.0
|
N
|
A:CYS264
|
4.1
|
49.2
|
1.0
|
CB
|
A:THR297
|
4.2
|
46.0
|
1.0
|
CG
|
A:TYR301
|
4.3
|
48.2
|
1.0
|
CE1
|
A:PHE294
|
4.4
|
40.9
|
1.0
|
CE2
|
A:PHE294
|
4.5
|
41.6
|
1.0
|
C
|
A:THR297
|
4.6
|
46.3
|
1.0
|
N
|
A:SER298
|
4.7
|
46.7
|
1.0
|
CB
|
A:TYR301
|
4.7
|
48.5
|
1.0
|
O
|
A:PHE294
|
4.8
|
45.1
|
1.0
|
O
|
A:THR297
|
4.8
|
46.0
|
1.0
|
CZ
|
A:TYR301
|
4.9
|
49.6
|
1.0
|
C
|
A:ILE263
|
5.0
|
48.8
|
1.0
|
CA
|
A:THR297
|
5.0
|
46.6
|
1.0
|
|
Mercury binding site 2 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 2 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg903
b:89.5
occ:0.75
|
SG
|
A:CYS222
|
2.3
|
75.9
|
1.0
|
O
|
A:CYS222
|
3.2
|
77.4
|
1.0
|
O
|
A:ALA132
|
3.4
|
61.7
|
1.0
|
C
|
A:CYS222
|
3.4
|
76.9
|
1.0
|
CB
|
A:CYS222
|
3.6
|
75.0
|
1.0
|
N
|
A:TYR223
|
3.7
|
78.4
|
1.0
|
CD2
|
A:LEU226
|
3.8
|
98.8
|
1.0
|
CA
|
A:TYR223
|
3.9
|
80.0
|
1.0
|
CA
|
A:ALA132
|
3.9
|
61.7
|
1.0
|
CD1
|
A:LEU226
|
4.0
|
98.8
|
1.0
|
C
|
A:ALA132
|
4.1
|
61.9
|
1.0
|
CA
|
A:CYS222
|
4.2
|
75.7
|
1.0
|
CB
|
A:ARG135
|
4.2
|
65.8
|
1.0
|
CB
|
A:ALA132
|
4.2
|
61.7
|
1.0
|
CG
|
A:LEU226
|
4.3
|
99.0
|
1.0
|
CG
|
A:ARG135
|
4.4
|
65.2
|
1.0
|
CB
|
A:LEU226
|
4.6
|
99.0
|
1.0
|
N
|
A:TYR136
|
4.7
|
71.8
|
1.0
|
CB
|
A:TYR223
|
4.7
|
79.9
|
1.0
|
O
|
A:ILE219
|
4.7
|
66.8
|
1.0
|
CB
|
A:TYR136
|
4.9
|
73.7
|
1.0
|
|
Mercury binding site 3 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 3 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg905
b:81.7
occ:0.58
|
O
|
A:HOH2061
|
2.5
|
54.0
|
1.0
|
SG
|
A:CYS316
|
2.5
|
62.7
|
1.0
|
O
|
A:GLN312
|
3.0
|
57.4
|
1.0
|
N
|
A:VAL337
|
3.5
|
91.6
|
1.0
|
N
|
A:CYS316
|
3.6
|
62.3
|
1.0
|
CB
|
A:CYS316
|
3.6
|
63.4
|
1.0
|
CG
|
A:GLN312
|
3.7
|
61.2
|
1.0
|
CG1
|
A:VAL337
|
3.7
|
89.1
|
1.0
|
CA
|
A:CYS316
|
3.8
|
63.9
|
1.0
|
O
|
A:VAL337
|
3.8
|
84.5
|
1.0
|
CA
|
A:THR336
|
3.9
|
96.5
|
1.0
|
C
|
A:THR336
|
4.0
|
94.1
|
1.0
|
CB
|
A:ASN315
|
4.0
|
59.0
|
1.0
|
C
|
A:GLN312
|
4.0
|
56.9
|
1.0
|
C
|
A:ASN315
|
4.3
|
60.4
|
1.0
|
CA
|
A:GLN312
|
4.3
|
57.8
|
1.0
|
CG2
|
A:THR336
|
4.3
|
97.2
|
1.0
|
CA
|
A:VAL337
|
4.4
|
88.7
|
1.0
|
CB
|
A:THR336
|
4.4
|
96.9
|
1.0
|
C
|
A:VAL337
|
4.5
|
86.5
|
1.0
|
CB
|
A:GLN312
|
4.6
|
58.8
|
1.0
|
CB
|
A:VAL337
|
4.7
|
88.8
|
1.0
|
CA
|
A:ASN315
|
4.7
|
58.6
|
1.0
|
CD
|
A:GLN312
|
4.7
|
62.6
|
1.0
|
NE2
|
A:GLN312
|
4.8
|
63.2
|
1.0
|
O
|
A:THR336
|
5.0
|
93.7
|
1.0
|
O
|
A:ASN315
|
5.0
|
61.1
|
1.0
|
|
Mercury binding site 4 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 4 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 4 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg902
b:86.1
occ:0.83
|
SG
|
B:CYS264
|
2.4
|
61.5
|
1.0
|
CB
|
B:CYS264
|
3.2
|
57.7
|
1.0
|
OG1
|
B:THR297
|
3.5
|
51.4
|
1.0
|
O
|
B:ALA260
|
3.5
|
58.6
|
1.0
|
CD2
|
B:TYR301
|
3.6
|
53.0
|
1.0
|
CA
|
B:CYS264
|
3.8
|
56.9
|
1.0
|
CE2
|
B:TYR301
|
4.0
|
54.6
|
1.0
|
N
|
B:CYS264
|
4.1
|
57.2
|
1.0
|
CG
|
B:TYR301
|
4.2
|
53.1
|
1.0
|
CZ
|
B:PHE294
|
4.2
|
46.9
|
1.0
|
C
|
B:ALA260
|
4.5
|
57.8
|
1.0
|
CB
|
B:TYR301
|
4.6
|
52.5
|
1.0
|
CE2
|
B:PHE294
|
4.6
|
47.1
|
1.0
|
C
|
B:ILE263
|
4.7
|
57.6
|
1.0
|
CB
|
B:THR297
|
4.7
|
50.2
|
1.0
|
CZ
|
B:TYR301
|
4.8
|
54.6
|
1.0
|
CE1
|
B:PHE294
|
4.9
|
47.4
|
1.0
|
CD1
|
B:TYR301
|
5.0
|
54.7
|
1.0
|
|
Mercury binding site 5 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 5 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 5 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg904
b:0.1
occ:0.66
|
SG
|
B:CYS222
|
2.1
|
85.8
|
1.0
|
O
|
B:CYS222
|
3.2
|
83.6
|
1.0
|
C
|
B:CYS222
|
3.4
|
83.7
|
1.0
|
O
|
B:ALA132
|
3.4
|
75.0
|
1.0
|
CB
|
B:CYS222
|
3.4
|
84.7
|
1.0
|
N
|
B:TYR223
|
3.7
|
84.1
|
1.0
|
CA
|
B:ALA132
|
3.8
|
73.8
|
1.0
|
CA
|
B:TYR223
|
3.9
|
85.0
|
1.0
|
C
|
B:ALA132
|
4.0
|
75.0
|
1.0
|
CA
|
B:CYS222
|
4.1
|
83.7
|
1.0
|
CB
|
B:ARG135
|
4.1
|
82.3
|
1.0
|
CB
|
B:ALA132
|
4.2
|
72.8
|
1.0
|
CD2
|
B:LEU226
|
4.2
|
0.0
|
1.0
|
CD1
|
B:LEU226
|
4.4
|
0.3
|
1.0
|
CG
|
B:ARG135
|
4.4
|
81.9
|
1.0
|
O
|
B:ILE219
|
4.6
|
73.1
|
1.0
|
CB
|
B:TYR223
|
4.6
|
83.9
|
1.0
|
CG
|
B:LEU226
|
4.8
|
0.7
|
1.0
|
N
|
B:TYR136
|
4.8
|
85.2
|
1.0
|
CB
|
B:LEU226
|
5.0
|
0.6
|
1.0
|
|
Mercury binding site 6 out
of 6 in 2g87
Go back to
Mercury Binding Sites List in 2g87
Mercury binding site 6 out
of 6 in the Crystallographic Model of Bathorhodopsin
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 6 of Crystallographic Model of Bathorhodopsin within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Hg906
b:0.1
occ:0.36
|
O
|
B:VAL337
|
2.0
|
0.9
|
1.0
|
O
|
B:THR336
|
2.2
|
0.0
|
1.0
|
SG
|
B:CYS316
|
2.3
|
69.8
|
1.0
|
CB
|
B:CYS316
|
2.4
|
69.4
|
1.0
|
CA
|
B:CYS316
|
3.1
|
69.7
|
1.0
|
ND1
|
B:HIS65
|
3.1
|
75.8
|
1.0
|
C
|
B:THR336
|
3.1
|
0.2
|
1.0
|
C
|
B:VAL337
|
3.2
|
0.5
|
1.0
|
OG
|
B:SER338
|
3.5
|
0.4
|
1.0
|
CE1
|
B:HIS65
|
3.8
|
75.7
|
1.0
|
N
|
B:VAL337
|
3.9
|
0.9
|
1.0
|
CA
|
B:VAL337
|
4.1
|
0.2
|
1.0
|
N
|
B:CYS316
|
4.1
|
69.7
|
1.0
|
CA
|
B:THR336
|
4.1
|
0.6
|
1.0
|
C
|
B:CYS316
|
4.1
|
69.5
|
1.0
|
O
|
B:CYS316
|
4.2
|
69.5
|
1.0
|
CG
|
B:HIS65
|
4.2
|
75.6
|
1.0
|
N
|
B:SER338
|
4.2
|
1.0
|
1.0
|
CE
|
B:LYS67
|
4.4
|
82.7
|
1.0
|
CA
|
B:SER338
|
4.5
|
0.8
|
1.0
|
CB
|
B:HIS65
|
4.6
|
75.4
|
1.0
|
CB
|
B:SER338
|
4.6
|
0.8
|
1.0
|
CB
|
B:THR336
|
4.7
|
0.4
|
1.0
|
CG2
|
B:THR342
|
4.7
|
0.0
|
1.0
|
NZ
|
B:LYS67
|
4.8
|
83.9
|
1.0
|
OG1
|
B:THR319
|
4.9
|
76.9
|
1.0
|
C
|
B:ASN315
|
4.9
|
69.8
|
1.0
|
O
|
B:GLN312
|
5.0
|
69.4
|
1.0
|
|
Reference:
H.Nakamichi,
T.Okada.
Crystallographic Analysis of Primary Visual Photochemistry Angew.Chem.Int.Ed.Engl. V. 45 4270 2006.
ISSN: ISSN 1433-7851
PubMed: 16586416
DOI: 10.1002/ANIE.200600595
Page generated: Sun Aug 11 02:35:00 2024
|