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Mercury in PDB 4jss: Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor

Enzymatic activity of Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor

All present enzymatic activity of Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor, PDB code: 4jss was solved by D.P.Martin, Z.S.Hann, S.M.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.76 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.855, 41.576, 72.369, 90.00, 104.43, 90.00
R / Rfree (%) 19.1 / 22.6

Other elements in 4jss:

The structure of Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor (pdb code 4jss). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor, PDB code: 4jss:

Mercury binding site 1 out of 1 in 4jss

Go back to Mercury Binding Sites List in 4jss
Mercury binding site 1 out of 1 in the Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II H94D Bound to A Bidentate Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:13.1
occ:0.60
HG A:MBO302 0.0 13.1 0.6
SG A:CYS206 2.1 8.2 0.6
CE5 A:MBO302 2.2 2.0 0.6
O A:GLN137 3.0 7.3 1.0
O A:GLU205 3.1 7.6 1.0
CE2 A:MBO302 3.2 11.5 0.6
CE1 A:MBO302 3.2 11.9 0.6
CB A:CYS206 3.2 7.4 0.6
CB A:CYS206 3.3 7.2 0.4
C A:GLN137 3.4 8.7 1.0
C A:GLU205 3.4 6.7 1.0
CA A:CYS206 3.5 7.9 0.6
CA A:CYS206 3.5 7.7 0.4
N A:GLN137 3.7 8.3 1.0
N A:CYS206 3.7 6.0 1.0
O A:VAL135 3.7 16.6 1.0
O A:HOH493 4.0 20.7 1.0
N A:PRO138 4.0 8.8 1.0
C A:GLN136 4.1 11.8 1.0
N A:GLU205 4.1 6.5 1.0
CA A:PRO138 4.1 10.1 1.0
CA A:GLN137 4.1 10.0 1.0
C A:VAL135 4.2 10.4 1.0
CA A:GLU205 4.3 6.3 1.0
CE4 A:MBO302 4.5 14.8 0.6
CE3 A:MBO302 4.5 13.8 0.6
CA A:GLN136 4.5 11.4 1.0
SG A:CYS206 4.6 8.6 0.4
O A:GLN136 4.6 13.2 1.0
N A:GLN136 4.7 10.7 1.0
C A:LEU204 4.8 8.4 1.0
C A:CYS206 4.9 7.9 1.0
CB A:GLU205 4.9 7.5 1.0
CB A:LEU204 4.9 5.8 1.0
CA A:VAL135 5.0 9.8 1.0
CD A:PRO138 5.0 10.3 1.0

Reference:

D.P.Martin, Z.S.Hann, S.M.Cohen. Metalloprotein-Inhibitor Binding: Human Carbonic Anhydrase II As A Model For Probing Metal-Ligand Interactions in A Metalloprotein Active Site. Inorg.Chem. V. 52 12207 2013.
ISSN: ISSN 0020-1669
PubMed: 23706138
DOI: 10.1021/IC400295F
Page generated: Sun Dec 13 19:11:18 2020

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