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Mercury in PDB 5thn: Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2

Enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2

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

Protein crystallography data

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2, PDB code: 5thn 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 / 1.33
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.982, 41.108, 71.670, 90.00, 104.23, 90.00
R / Rfree (%) 17.6 / 20.6

Other elements in 5thn:

The structure of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2 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-Triene-1-Thione Bound to Human Carbonic Anhydrase 2 (pdb code 5thn). 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-Triene-1-Thione Bound to Human Carbonic Anhydrase 2, PDB code: 5thn:

Mercury binding site 1 out of 1 in 5thn

Go back to Mercury Binding Sites List in 5thn
Mercury binding site 1 out of 1 in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2


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-Triene-1-Thione Bound to Human Carbonic Anhydrase 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg302

b:11.9
occ:0.60
HG A:MBO302 0.0 11.9 0.6
CE1 A:MBO302 2.2 12.0 0.6
SG A:CYS206 2.3 7.3 0.5
O A:VAL135 2.5 16.2 1.0
CB A:CYS206 2.8 6.7 0.5
CE6 A:MBO302 3.0 9.8 0.6
O A:GLN137 3.1 7.5 1.0
CE2 A:MBO302 3.1 11.7 0.6
CB A:CYS206 3.2 6.7 0.5
C A:VAL135 3.4 11.8 1.0
CA A:CYS206 3.4 5.8 0.5
CA A:CYS206 3.4 5.8 0.5
N A:GLN137 3.5 9.1 1.0
N A:CYS206 3.6 6.1 0.5
N A:CYS206 3.6 6.1 0.5
SG A:CYS206 3.7 7.1 0.5
C A:GLN137 3.7 7.5 1.0
C A:GLU205 3.7 7.7 1.0
O A:GLU205 3.7 8.3 1.0
O A:HOH558 3.8 18.1 1.0
C A:GLN136 3.8 13.0 1.0
CB A:LEU204 4.0 8.9 1.0
N A:GLN136 4.1 10.9 1.0
CA A:GLN136 4.1 13.1 1.0
CA A:VAL135 4.1 10.4 1.0
N A:GLU205 4.1 7.2 1.0
CA A:GLN137 4.2 8.5 1.0
CE5 A:MBO302 4.3 12.6 0.6
CE3 A:MBO302 4.4 12.0 0.6
N A:PRO138 4.5 8.1 1.0
C A:LEU204 4.5 6.3 1.0
CA A:GLU205 4.5 6.9 1.0
O A:ALA134 4.6 6.9 1.0
O A:GLN136 4.6 13.1 1.0
CA A:PRO138 4.7 7.9 1.0
CA A:LEU204 4.8 7.2 1.0
C A:CYS206 4.8 5.8 0.5
CE4 A:MBO302 4.8 14.2 0.6
CB A:VAL135 4.9 10.1 1.0
C A:CYS206 4.9 5.7 0.5
CG A:LEU204 5.0 10.8 1.0
O A:LEU204 5.0 7.0 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: Sun Dec 13 19:13:14 2020

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