Zinc 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:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc 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:

Zinc binding site 1 out of 1 in 5thi

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

b:7.2
occ:0.90
 OA2 A:0TR302 1.9 14.1 0.9
NE2 A:HIS96 2.0 6.5 1.0
NE2 A:HIS94 2.1 6.2 1.0
ND1 A:HIS119 2.1 7.5 1.0
OA1 A:0TR302 2.4 23.7 0.9
CA2 A:0TR302 2.9 26.9 0.9
CE1 A:HIS96 3.0 7.0 1.0
CE1 A:HIS119 3.0 6.8 1.0
CD2 A:HIS96 3.0 7.1 1.0
CD2 A:HIS94 3.0 8.3 1.0
CE1 A:HIS94 3.1 6.5 1.0
CA1 A:0TR302 3.1 26.7 0.9
CG A:HIS119 3.2 6.6 1.0
CB A:HIS119 3.6 6.8 1.0
OG1 A:THR199 3.8 9.3 1.0
O A:HOH417 3.8 25.1 1.0
OE1 A:GLU106 4.0 7.5 1.0
ND1 A:HIS96 4.1 7.7 1.0
CG A:HIS96 4.2 6.8 1.0
CA3 A:0TR302 4.2 26.9 0.9
NE2 A:HIS119 4.2 6.7 1.0
ND1 A:HIS94 4.2 6.4 1.0
CG A:HIS94 4.2 6.5 1.0
CD2 A:HIS119 4.2 6.0 1.0
O A:HOH588 4.4 17.9 1.0
CA6 A:0TR302 4.4 27.9 0.9
CD A:GLU106 4.9 7.6 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: Wed Dec 16 10:55:46 2020

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