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Mercury in PDB 8ogd: Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate

Enzymatic activity of Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate

All present enzymatic activity of Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate:
4.2.1.1; 4.2.1.69;

Protein crystallography data

The structure of Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate, PDB code: 8ogd was solved by J.M.Silva, L.Cerofolini, A.L.Carvalho, E.Ravera, M.Fragai, G.Parigi, A.L.Macedo, C.F.G.C.Geraldes, C.Luchinat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.77 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.028, 41.333, 72.25, 90, 104.43, 90
R / Rfree (%) 17.1 / 19.8

Other elements in 8ogd:

The structure of Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate (pdb code 8ogd). 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 Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate, PDB code: 8ogd:

Mercury binding site 1 out of 1 in 8ogd

Go back to Mercury Binding Sites List in 8ogd
Mercury binding site 1 out of 1 in the Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of Zinc(II) Double Mutant Human Carbonic Anhydrase II Bound to Thiocyanate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg301

b:16.1
occ:1.00
 HG A:HGB301 0.0 16.1 1.0
HG A:CYS206 1.3 16.2 1.0
C7 A:HGB301 2.1 17.0 1.0
SG A:CYS206 2.3 13.5 1.0
O A:HOH610 2.8 14.3 1.0
O A:GLN137 2.9 10.8 1.0
C5 A:HGB301 3.1 15.7 1.0
C6 A:HGB301 3.1 15.2 1.0
HC5 A:HGB301 3.1 18.8 1.0
HA A:CYS206 3.1 9.2 1.0
HC6 A:HGB301 3.1 18.2 1.0
O A:GLU205 3.3 8.8 1.0
CB A:CYS206 3.3 9.7 1.0
C A:GLN137 3.4 9.2 1.0
HA A:PRO138 3.5 11.7 1.0
H A:GLN137 3.5 16.5 1.0
C A:GLU205 3.5 8.1 1.0
CA A:CYS206 3.5 7.7 1.0
HB3 A:CYS206 3.6 11.6 1.0
N A:GLN137 3.6 13.8 1.0
N A:CYS206 3.7 8.1 1.0
O A:VAL135 3.9 10.8 1.0
HB3 A:LEU204 4.0 10.2 1.0
H A:GLU205 4.0 13.9 1.0
N A:PRO138 4.0 8.3 1.0
C A:GLN136 4.0 10.2 1.0
CA A:GLN137 4.0 7.7 1.0
O A:HOH621 4.1 11.8 1.0
HA A:GLN136 4.1 12.5 1.0
HB2 A:CYS206 4.2 11.6 1.0
CA A:PRO138 4.2 9.8 1.0
N A:GLU205 4.2 11.6 1.0
HA A:GLN137 4.3 9.2 1.0
H A:CYS206 4.3 9.7 1.0
C A:VAL135 4.3 13.4 1.0
C3 A:HGB301 4.4 21.4 1.0
C4 A:HGB301 4.4 21.5 1.0
CA A:GLU205 4.4 7.6 1.0
CA A:GLN136 4.5 10.4 1.0
O A:GLN136 4.5 7.3 1.0
HB2 A:GLU205 4.5 8.7 1.0
HA A:VAL135 4.6 15.0 1.0
HD3 A:PRO138 4.7 16.5 1.0
N A:GLN136 4.7 8.8 1.0
C A:LEU204 4.9 10.0 1.0
CB A:LEU204 4.9 8.6 1.0
CD A:PRO138 4.9 13.8 1.0
C2 A:HGB301 4.9 18.2 1.0
C A:CYS206 5.0 8.1 1.0

Reference:

J.M.Silva, L.Cerofolini, A.L.Carvalho, E.Ravera, M.Fragai, G.Parigi, A.L.Macedo, C.F.G.C.Geraldes, C.Luchinat. Elucidating the Concentration-Dependent Effects of Thiocyanate Binding to Carbonic Anhydrase. J.Inorg.Biochem. V. 244 12222 2023.
ISSN: ISSN 0162-0134
PubMed: 37068394
DOI: 10.1016/J.JINORGBIO.2023.112222
Page generated: Fri Aug 8 11:34:11 2025

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