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Zinc in PDB 6h36: The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide.

Enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide.

All present enzymatic activity of The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide.:
4.2.1.1;

Protein crystallography data

The structure of The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide., PDB code: 6h36 was solved by M.R.Buemi, A.Di Fiore, L.De Luca, S.Ferro, F.Mancuso, S.M.Monti, M.Buonanno, A.Angeli, E.Russo, G.De Sarro, C.T.Supuran, G.De Simone, R.Gitto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 31.10 / 1.85
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 66.020, 88.070, 43.960, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 23.3

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide. (pdb code 6h36). 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 The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide., PDB code: 6h36:

Zinc binding site 1 out of 1 in 6h36

Go back to Zinc Binding Sites List in 6h36
Zinc binding site 1 out of 1 in the The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Human Carbonic Anhydrase VII in Complex with 4-(4-Phenylpiperidine-1-Carbonyl)Benzenesulfonamide. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:13.6
occ:1.00
 N1 A:FKE302 2.0 9.0 1.0
NE2 A:HIS96 2.0 14.2 1.0
NE2 A:HIS94 2.0 12.6 1.0
ND1 A:HIS119 2.0 11.3 1.0
CE1 A:HIS119 3.0 11.1 1.0
CE1 A:HIS96 3.0 16.4 1.0
CE1 A:HIS94 3.0 11.8 1.0
O2 A:FKE302 3.0 10.1 1.0
CD2 A:HIS96 3.1 16.2 1.0
CD2 A:HIS94 3.1 12.0 1.0
S1 A:FKE302 3.1 12.3 1.0
CG A:HIS119 3.1 12.0 1.0
CB A:HIS119 3.5 11.7 1.0
OG1 A:THR199 3.9 12.8 1.0
OE1 A:GLU106 4.0 14.5 1.0
C1 A:FKE302 4.1 14.0 1.0
ND1 A:HIS96 4.1 12.3 1.0
NE2 A:HIS119 4.1 10.0 1.0
ND1 A:HIS94 4.2 10.6 1.0
CG A:HIS96 4.2 14.7 1.0
C6 A:FKE302 4.2 17.3 1.0
O1 A:FKE302 4.2 10.5 1.0
CG A:HIS94 4.2 11.9 1.0
CD2 A:HIS119 4.2 10.8 1.0
CD A:GLU106 4.8 16.8 1.0
CA A:HIS119 5.0 12.8 1.0

Reference:

M.R.Buemi, A.Di Fiore, L.De Luca, A.Angeli, F.Mancuso, S.Ferro, S.M.Monti, M.Buonanno, E.Russo, G.De Sarro, G.De Simone, C.T.Supuran, R.Gitto. Exploring Structural Properties of Potent Human Carbonic Anhydrase Inhibitors Bearing A 4-(Cycloalkylamino-1-Carbonyl)Benzenesulfonamide Moiety. Eur J Med Chem V. 163 443 2018.
ISSN: ISSN 1768-3254
PubMed: 30530195
DOI: 10.1016/J.EJMECH.2018.11.073
Page generated: Mon Oct 28 22:19:54 2024

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