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Zinc 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:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Triene-1-Thione Bound to Human Carbonic Anhydrase 2, PDB code: 5thn:

Zinc binding site 1 out of 1 in 5thn

Go back to Zinc Binding Sites List in 5thn
Zinc 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 Zinc with other atoms in the Zn 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:Zn301

b:7.3
occ:1.00
 NE2 A:HIS96 2.0 5.9 1.0
NE2 A:HIS94 2.1 5.4 1.0
ND1 A:HIS119 2.1 5.5 1.0
SAH A:7CZ305 2.3 14.6 1.0
OAI A:7CZ305 2.5 15.0 1.0
CE1 A:HIS119 3.0 6.0 1.0
CD2 A:HIS96 3.0 5.6 1.0
CD2 A:HIS94 3.0 5.8 1.0
CE1 A:HIS94 3.0 5.3 1.0
CE1 A:HIS96 3.1 5.5 1.0
CAF A:7CZ305 3.1 10.7 1.0
CAE A:7CZ305 3.2 14.2 1.0
CG A:HIS119 3.2 5.0 1.0
OG1 A:THR199 3.6 6.2 1.0
CB A:HIS119 3.6 4.9 1.0
OE1 A:GLU106 4.0 6.5 1.0
NE2 A:HIS119 4.1 5.5 1.0
O A:HOH532 4.1 11.9 1.0
ND1 A:HIS94 4.2 6.0 1.0
ND1 A:HIS96 4.2 5.4 1.0
CG A:HIS94 4.2 5.5 1.0
CG A:HIS96 4.2 5.0 1.0
CD2 A:HIS119 4.3 5.6 1.0
CAA A:7CZ305 4.4 17.2 1.0
CAG A:7CZ305 4.4 14.3 1.0
O A:HOH543 4.5 18.7 1.0
CB A:THR199 4.9 5.6 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: Mon Oct 28 08:32:31 2024

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