Mercury in PDB 2o9g: Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
Protein crystallography data
The structure of Crystal Structure of Aqpz Mutant L170C Complexed with Mercury., PDB code: 2o9g
was solved by
D.F.Savage,
R.M.Stroud,
Center For Structures Of Membrane Proteins(Csmp),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
64.42 /
1.90
|
Space group
|
I 4
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.156,
91.156,
77.145,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.6 /
19.5
|
Mercury Binding Sites:
The binding sites of Mercury atom in the Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
(pdb code 2o9g). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 4 binding sites of Mercury where determined in the
Crystal Structure of Aqpz Mutant L170C Complexed with Mercury., PDB code: 2o9g:
Jump to Mercury binding site number:
1;
2;
3;
4;
Mercury binding site 1 out
of 4 in 2o9g
Go back to
Mercury Binding Sites List in 2o9g
Mercury binding site 1 out
of 4 in the Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 1 of Crystal Structure of Aqpz Mutant L170C Complexed with Mercury. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg303
b:32.6
occ:0.40
|
HG
|
A:HG304
|
2.5
|
34.0
|
0.2
|
CG2
|
A:VAL185
|
2.8
|
25.3
|
1.0
|
CE2
|
A:PHE145
|
3.5
|
17.1
|
1.0
|
SG
|
A:CYS170
|
3.7
|
22.8
|
1.0
|
HG
|
A:HG305
|
3.7
|
48.2
|
0.2
|
CZ
|
A:PHE145
|
3.7
|
17.9
|
1.0
|
CD2
|
A:PHE145
|
3.8
|
17.2
|
1.0
|
CB
|
A:CYS170
|
4.0
|
18.9
|
1.0
|
CD1
|
A:ILE173
|
4.0
|
18.4
|
1.0
|
CA
|
A:CYS170
|
4.0
|
17.5
|
1.0
|
CE1
|
A:PHE145
|
4.1
|
14.0
|
1.0
|
CB
|
A:VAL185
|
4.1
|
23.1
|
1.0
|
HG
|
A:HG306
|
4.1
|
38.4
|
0.2
|
CG
|
A:PHE145
|
4.2
|
16.9
|
1.0
|
CD1
|
A:PHE145
|
4.3
|
16.3
|
1.0
|
CG2
|
A:ILE173
|
4.4
|
17.9
|
1.0
|
CB
|
A:ILE173
|
4.6
|
15.5
|
1.0
|
NE2
|
A:HIS174
|
4.6
|
20.9
|
1.0
|
O
|
A:VAL185
|
4.7
|
22.0
|
1.0
|
O
|
A:CYS170
|
4.7
|
16.4
|
1.0
|
CD2
|
A:HIS174
|
4.8
|
17.8
|
1.0
|
C
|
A:CYS170
|
4.9
|
16.4
|
1.0
|
ND2
|
A:ASN63
|
4.9
|
14.2
|
1.0
|
O
|
A:SER184
|
4.9
|
23.9
|
1.0
|
CG1
|
A:VAL185
|
4.9
|
22.4
|
1.0
|
N
|
A:CYS170
|
4.9
|
18.0
|
1.0
|
CG1
|
A:ILE173
|
4.9
|
15.8
|
1.0
|
|
Mercury binding site 2 out
of 4 in 2o9g
Go back to
Mercury Binding Sites List in 2o9g
Mercury binding site 2 out
of 4 in the Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 2 of Crystal Structure of Aqpz Mutant L170C Complexed with Mercury. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg304
b:34.0
occ:0.23
|
HG
|
A:HG305
|
2.3
|
48.2
|
0.2
|
HG
|
A:HG306
|
2.4
|
38.4
|
0.2
|
HG
|
A:HG303
|
2.5
|
32.6
|
0.4
|
SG
|
A:CYS170
|
2.7
|
22.8
|
1.0
|
CB
|
A:CYS170
|
3.5
|
18.9
|
1.0
|
CG2
|
A:VAL47
|
3.8
|
18.8
|
1.0
|
CZ
|
A:PHE145
|
3.9
|
17.9
|
1.0
|
CE2
|
A:PHE145
|
4.0
|
17.1
|
1.0
|
O
|
A:HOH444
|
4.2
|
34.3
|
1.0
|
CA
|
A:CYS170
|
4.5
|
17.5
|
1.0
|
CD1
|
A:LEU15
|
4.5
|
19.3
|
1.0
|
ND2
|
A:ASN63
|
4.6
|
14.2
|
1.0
|
CG2
|
A:VAL185
|
4.7
|
25.3
|
1.0
|
CE1
|
A:PHE145
|
4.7
|
14.0
|
1.0
|
NE2
|
A:HIS174
|
4.8
|
20.9
|
1.0
|
ND2
|
A:ASN186
|
4.8
|
18.9
|
1.0
|
CD2
|
A:PHE145
|
5.0
|
17.2
|
1.0
|
|
Mercury binding site 3 out
of 4 in 2o9g
Go back to
Mercury Binding Sites List in 2o9g
Mercury binding site 3 out
of 4 in the Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 3 of Crystal Structure of Aqpz Mutant L170C Complexed with Mercury. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg305
b:48.2
occ:0.20
|
HG
|
A:HG304
|
2.3
|
34.0
|
0.2
|
O
|
A:HOH328
|
3.0
|
39.6
|
1.0
|
HG
|
A:HG306
|
3.5
|
38.4
|
0.2
|
HG
|
A:HG303
|
3.7
|
32.6
|
0.4
|
CD2
|
A:LEU15
|
3.7
|
24.3
|
1.0
|
SG
|
A:CYS170
|
3.8
|
22.8
|
1.0
|
NE2
|
A:HIS174
|
3.8
|
20.9
|
1.0
|
ND2
|
A:ASN186
|
3.9
|
18.9
|
1.0
|
CB
|
A:ASN186
|
4.0
|
18.6
|
1.0
|
CD1
|
A:PHE43
|
4.1
|
15.9
|
1.0
|
CD1
|
A:LEU15
|
4.1
|
19.3
|
1.0
|
O
|
A:SER184
|
4.2
|
23.9
|
1.0
|
CG
|
A:LEU15
|
4.2
|
20.9
|
1.0
|
CG
|
A:ASN186
|
4.5
|
20.2
|
1.0
|
CE1
|
A:HIS174
|
4.6
|
17.6
|
1.0
|
CG2
|
A:VAL185
|
4.6
|
25.3
|
1.0
|
CE1
|
A:PHE43
|
4.6
|
17.8
|
1.0
|
CD2
|
A:HIS174
|
4.8
|
17.8
|
1.0
|
ND2
|
A:ASN63
|
4.9
|
14.2
|
1.0
|
CG
|
A:PHE43
|
4.9
|
17.4
|
1.0
|
|
Mercury binding site 4 out
of 4 in 2o9g
Go back to
Mercury Binding Sites List in 2o9g
Mercury binding site 4 out
of 4 in the Crystal Structure of Aqpz Mutant L170C Complexed with Mercury.
Mono view
Stereo pair view
|
A full contact list of Mercury with other atoms in the Hg binding
site number 4 of Crystal Structure of Aqpz Mutant L170C Complexed with Mercury. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Hg306
b:38.4
occ:0.17
|
O
|
A:HOH444
|
2.3
|
34.3
|
1.0
|
HG
|
A:HG304
|
2.4
|
34.0
|
0.2
|
ND2
|
A:ASN63
|
3.1
|
14.2
|
1.0
|
HG
|
A:HG305
|
3.5
|
48.2
|
0.2
|
ND2
|
A:ASN186
|
3.6
|
18.9
|
1.0
|
CE2
|
A:PHE145
|
3.6
|
17.1
|
1.0
|
CB
|
A:ASN63
|
3.7
|
17.2
|
1.0
|
CD1
|
A:LEU15
|
3.7
|
19.3
|
1.0
|
CZ
|
A:PHE145
|
3.8
|
17.9
|
1.0
|
CG
|
A:ASN63
|
3.9
|
18.2
|
1.0
|
CG2
|
A:VAL47
|
4.0
|
18.8
|
1.0
|
HG
|
A:HG303
|
4.1
|
32.6
|
0.4
|
O
|
A:HIS61
|
4.4
|
18.7
|
1.0
|
CG
|
A:ASN186
|
4.5
|
20.2
|
1.0
|
O
|
A:HOH443
|
4.6
|
38.2
|
1.0
|
O
|
A:PHE62
|
4.6
|
17.8
|
1.0
|
CB
|
A:ASN186
|
4.7
|
18.6
|
1.0
|
CD2
|
A:PHE145
|
4.8
|
17.2
|
1.0
|
CG2
|
A:VAL66
|
4.9
|
12.8
|
1.0
|
CG
|
A:LEU15
|
4.9
|
20.9
|
1.0
|
CA
|
A:ASN63
|
4.9
|
17.0
|
1.0
|
SG
|
A:CYS170
|
5.0
|
22.8
|
1.0
|
C
|
A:PHE62
|
5.0
|
17.4
|
1.0
|
|
Reference:
D.F.Savage,
R.M.Stroud.
Structural Basis of Aquaporin Inhibition By Mercury. J.Mol.Biol. V. 368 607 2007.
ISSN: ISSN 0022-2836
PubMed: 17376483
DOI: 10.1016/J.JMB.2007.02.070
Page generated: Sun Aug 11 02:53:29 2024
|