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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

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