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

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

All present enzymatic activity of Crystal Structure of 2-Hydroxycyclohepta-2,4,6-Trien-1-One Bound to Human Carbonic Anhydrase 2:
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, PDB code: 5thj 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 (°) 42.283, 41.340, 71.848, 90.00, 104.00, 90.00
R / Rfree (%) 15.4 / 18.9

Other elements in 5thj:

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

Zinc binding site 1 out of 1 in 5thj

Go back to Zinc Binding Sites List in 5thj
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


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:7.3
occ:1.00
 NE2 A:HIS94 2.0 5.5 1.0
NE2 A:HIS96 2.1 5.7 1.0
OA2 A:0TR302 2.1 14.0 1.0
ND1 A:HIS119 2.1 5.2 1.0
OA1 A:0TR302 2.3 14.3 1.0
CA2 A:0TR302 2.9 16.7 1.0
CA1 A:0TR302 2.9 15.4 1.0
CE1 A:HIS94 3.0 5.7 1.0
CE1 A:HIS119 3.0 4.7 1.0
CD2 A:HIS94 3.1 6.0 1.0
CD2 A:HIS96 3.1 5.0 1.0
CE1 A:HIS96 3.1 5.1 1.0
CG A:HIS119 3.2 4.7 1.0
CB A:HIS119 3.6 4.6 1.0
O A:HOH457 3.7 11.5 1.0
OG1 A:THR199 3.9 6.9 1.0
O A:HOH580 4.1 11.1 1.0
ND1 A:HIS94 4.1 5.7 1.0
CA3 A:0TR302 4.1 19.2 1.0
NE2 A:HIS119 4.1 4.5 1.0
CG A:HIS94 4.2 5.3 1.0
OE1 A:GLU106 4.2 5.7 1.0
ND1 A:HIS96 4.2 4.7 1.0
CG A:HIS96 4.2 4.7 1.0
CA6 A:0TR302 4.2 16.9 1.0
CD2 A:HIS119 4.3 4.6 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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