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Mercury in PDB 2o9e: Crystal Structure of Aqpz Mutant T183C Complexed with Mercury

Protein crystallography data

The structure of Crystal Structure of Aqpz Mutant T183C Complexed with Mercury, PDB code: 2o9e 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 / 2.20
Space group I 4
Cell size a, b, c (Å), α, β, γ (°) 91.103, 91.103, 77.944, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 24.3

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of Aqpz Mutant T183C Complexed with Mercury (pdb code 2o9e). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 3 binding sites of Mercury where determined in the Crystal Structure of Aqpz Mutant T183C Complexed with Mercury, PDB code: 2o9e:
Jump to Mercury binding site number: 1; 2; 3;

Mercury binding site 1 out of 3 in 2o9e

Go back to Mercury Binding Sites List in 2o9e
Mercury binding site 1 out of 3 in the Crystal Structure of Aqpz Mutant T183C 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 T183C Complexed with Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg232

b:54.2
occ:0.24
O A:SER184 3.1 41.0 1.0
NE2 A:HIS174 3.6 28.9 1.0
CB A:ASN186 3.7 32.1 1.0
CD1 A:PHE43 3.9 27.6 1.0
O A:HOH265 4.0 28.4 1.0
CD2 A:LEU170 4.0 24.1 1.0
CE1 A:PHE43 4.0 26.3 1.0
CD1 A:LEU170 4.1 28.3 1.0
CD2 A:LEU15 4.1 30.9 1.0
CE1 A:HIS174 4.2 27.4 1.0
CD A:ARG189 4.3 43.8 1.0
C A:SER184 4.4 39.5 1.0
ND2 A:ASN186 4.4 30.9 1.0
CG A:ASN186 4.5 33.0 1.0
CG A:ARG189 4.5 37.6 1.0
CB A:ARG189 4.6 35.8 1.0
CG A:LEU170 4.6 27.2 1.0
CG2 A:VAL185 4.7 35.1 1.0
N A:ASN186 4.8 33.2 1.0
CD2 A:HIS174 4.8 25.6 1.0
CG A:PHE43 4.8 26.4 1.0
CD1 A:LEU15 4.8 31.3 1.0
CA A:ASN186 4.9 32.3 1.0
CG A:LEU15 4.9 31.0 1.0

Mercury binding site 2 out of 3 in 2o9e

Go back to Mercury Binding Sites List in 2o9e
Mercury binding site 2 out of 3 in the Crystal Structure of Aqpz Mutant T183C 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 T183C Complexed with Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg233

b:54.0
occ:0.32
OE1 A:GLU138 2.5 45.8 1.0
CD A:GLU138 3.1 47.4 1.0
OG A:SER177 3.1 35.9 1.0
CG1 A:VAL185 3.4 33.3 1.0
OE2 A:GLU138 3.6 49.5 1.0
CB A:SER177 3.6 31.8 1.0
CD1 A:LEU141 3.8 23.4 1.0
CG A:GLU138 3.9 42.4 1.0
SG A:CYS183 4.0 40.4 1.0
CA A:GLU138 4.0 36.8 1.0
N A:SER184 4.1 39.2 1.0
OG1 A:THR181 4.2 36.9 1.0
CB A:LEU141 4.2 26.6 1.0
CA A:CYS183 4.2 38.0 1.0
N A:GLU138 4.2 34.9 1.0
CG1 A:VAL137 4.2 32.1 1.0
CG2 A:ILE173 4.4 21.1 1.0
O A:VAL137 4.4 34.1 1.0
C A:VAL137 4.4 34.4 1.0
CB A:GLU138 4.4 37.1 1.0
N A:VAL185 4.5 37.4 1.0
CG A:LEU141 4.5 27.5 1.0
CB A:CYS183 4.5 38.3 1.0
C A:CYS183 4.7 38.4 1.0
CB A:VAL185 4.8 36.0 1.0

Mercury binding site 3 out of 3 in 2o9e

Go back to Mercury Binding Sites List in 2o9e
Mercury binding site 3 out of 3 in the Crystal Structure of Aqpz Mutant T183C 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 T183C Complexed with Mercury within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg234

b:76.1
occ:0.27
CG A:MET131 3.4 45.4 1.0
SD A:MET131 3.7 48.9 1.0
CD2 A:LEU135 3.7 39.4 1.0
CB A:MET131 4.0 44.7 1.0
CE A:MET131 4.1 46.8 1.0
C A:MET131 4.1 43.4 1.0
O A:MET131 4.1 43.4 1.0
N A:LEU132 4.1 42.6 1.0
CA A:LEU132 4.1 42.1 1.0
CB A:LEU135 4.6 38.2 1.0
CB A:LEU132 4.6 42.0 1.0
CA A:MET131 4.7 44.8 1.0
CD1 A:LEU132 4.8 41.5 1.0
CG A:LEU135 4.8 38.4 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: Wed Oct 28 18:41:52 2020

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