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Mercury in PDB 4jsa: Benzenesulfonamide Complexed with Hcaii H94D

Enzymatic activity of Benzenesulfonamide Complexed with Hcaii H94D

All present enzymatic activity of Benzenesulfonamide Complexed with Hcaii H94D:
4.2.1.1;

Protein crystallography data

The structure of Benzenesulfonamide Complexed with Hcaii H94D, PDB code: 4jsa 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) 40.73 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.021, 41.389, 72.050, 90.00, 104.23, 90.00
R / Rfree (%) 17.8 / 21.7

Other elements in 4jsa:

The structure of Benzenesulfonamide Complexed with Hcaii H94D also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Benzenesulfonamide Complexed with Hcaii H94D (pdb code 4jsa). 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 Benzenesulfonamide Complexed with Hcaii H94D, PDB code: 4jsa:

Mercury binding site 1 out of 1 in 4jsa

Go back to Mercury Binding Sites List in 4jsa
Mercury binding site 1 out of 1 in the Benzenesulfonamide Complexed with Hcaii H94D


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Benzenesulfonamide Complexed with Hcaii H94D within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:21.9
occ:0.60
HG A:MBO302 0.0 21.9 0.6
CE5 A:MBO302 2.3 2.3 0.6
SG A:CYS206 2.8 10.3 0.4
O A:GLN137 3.0 8.5 1.0
CE2 A:MBO302 3.0 17.3 0.6
O A:VAL135 3.1 16.2 1.0
O A:GLU205 3.2 8.1 1.0
CB A:CYS206 3.2 8.6 0.6
CB A:CYS206 3.3 7.8 0.4
C A:GLN137 3.3 8.4 1.0
CE1 A:MBO302 3.4 14.4 0.6
N A:GLN137 3.5 9.3 1.0
CA A:CYS206 3.5 7.0 0.6
CA A:CYS206 3.5 6.8 0.4
C A:GLU205 3.5 4.9 1.0
N A:CYS206 3.7 5.6 1.0
C A:GLN136 3.8 14.5 1.0
O A:HOH438 3.8 18.8 1.0
N A:PRO138 3.9 9.6 1.0
CA A:GLN137 4.0 9.8 1.0
C A:VAL135 4.0 14.0 1.0
N A:GLU205 4.1 6.7 1.0
CA A:PRO138 4.2 7.6 1.0
CA A:GLN136 4.3 14.0 1.0
CA A:GLU205 4.4 5.8 1.0
O A:GLN136 4.4 15.1 1.0
CE4 A:MBO302 4.4 19.7 0.6
SG A:CYS206 4.4 11.3 0.6
N A:GLN136 4.6 12.0 1.0
CE3 A:MBO302 4.7 16.7 0.6
CB A:LEU204 4.8 7.3 1.0
CD A:PRO138 4.8 12.8 1.0
C A:LEU204 4.8 6.7 1.0
C A:CYS206 4.9 6.4 1.0
CA A:VAL135 4.9 11.6 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 19:11:16 2020

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