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Mercury in PDB 5thi: Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G

Enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G

All present enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G, PDB code: 5thi was solved by B.Dick, S.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.186, 41.368, 71.727, 90.00, 104.20, 90.00
R / Rfree (%) 16.9 / 19.6

Other elements in 5thi:

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G (pdb code 5thi). 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 Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G, PDB code: 5thi:

Mercury binding site 1 out of 1 in 5thi

Go back to Mercury Binding Sites List in 5thi
Mercury binding site 1 out of 1 in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G


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 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2 L198G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg304

b:12.3
occ:0.80
 HG A:MBO304 0.0 12.3 0.8
CE1 A:MBO304 2.1 11.3 0.8
SG A:CYS206 2.3 11.8 1.0
O A:GLN137 2.9 8.0 1.0
O A:VAL135 2.9 11.4 1.0
CE2 A:MBO304 3.0 9.3 0.8
CE6 A:MBO304 3.1 12.0 0.8
CB A:CYS206 3.3 8.9 1.0
CA A:CYS206 3.6 7.5 1.0
O A:GLU205 3.6 10.3 1.0
N A:GLN137 3.6 8.7 1.0
C A:VAL135 3.6 10.2 1.0
C A:GLN137 3.6 8.9 1.0
C A:GLU205 3.6 9.4 1.0
N A:CYS206 3.7 7.5 1.0
O A:HOH548 3.9 19.5 1.0
N A:GLU205 4.0 9.3 1.0
C A:GLN136 4.1 9.6 1.0
CB A:LEU204 4.1 14.2 1.0
CA A:VAL135 4.2 8.8 1.0
CA A:GLN137 4.2 9.7 1.0
N A:GLN136 4.3 9.9 1.0
CA A:GLN136 4.3 11.1 1.0
CE3 A:MBO304 4.4 12.1 0.8
CE5 A:MBO304 4.4 14.2 0.8
C A:LEU204 4.4 10.1 1.0
CA A:GLU205 4.4 8.7 1.0
N A:PRO138 4.5 8.9 1.0
CA A:PRO138 4.7 8.3 1.0
O A:ALA134 4.7 9.0 1.0
CA A:LEU204 4.8 11.3 1.0
O A:GLN136 4.8 11.5 1.0
CE4 A:MBO304 4.9 14.1 0.8
O A:HOH482 4.9 19.9 1.0
CB A:VAL135 4.9 10.6 1.0
O A:LEU204 5.0 8.2 1.0
CG A:LEU204 5.0 15.7 1.0

Reference:

B.L.Dick, A.Patel, J.A.Mccammon, S.M.Cohen. Effect of Donor Atom Identity on Metal-Binding Pharmacophore Coordination. J. Biol. Inorg. Chem. V. 22 605 2017.
ISSN: ESSN 1432-1327
PubMed: 28389830
DOI: 10.1007/S00775-017-1454-3
Page generated: Fri Aug 8 10:58:47 2025

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