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Zinc in PDB 3s78: The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase

Enzymatic activity of The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase

All present enzymatic activity of The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase:
4.2.1.1;

Protein crystallography data

The structure of The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase, PDB code: 3s78 was solved by P.W.Snyder, A.Heroux, G.W.Whitesides, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.62 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.985, 40.958, 71.637, 90.00, 104.27, 90.00
R / Rfree (%) 17.3 / 22.6

Zinc Binding Sites:

The binding sites of Zinc atom in the The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase (pdb code 3s78). 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 Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase, PDB code: 3s78:

Zinc binding site 1 out of 1 in 3s78

Go back to Zinc Binding Sites List in 3s78
Zinc binding site 1 out of 1 in the The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Origin of the Hydrophobic Effect in the Molecular Recognition of Arylsulfonamides By Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn262

b:16.2
occ:1.00
 ND1 B:HIS119 2.0 16.1 1.0
NH B:EVJ1 2.0 15.1 1.0
NE2 B:HIS94 2.0 15.2 1.0
NE2 B:HIS96 2.0 17.9 1.0
CE1 B:HIS119 2.9 19.0 1.0
CD2 B:HIS96 3.0 17.4 1.0
CD2 B:HIS94 3.0 16.4 1.0
CG B:HIS119 3.0 15.1 1.0
CE1 B:HIS94 3.0 14.6 1.0
CE1 B:HIS96 3.1 16.3 1.0
S B:EVJ1 3.1 16.2 1.0
O1 B:EVJ1 3.1 13.0 1.0
CB B:HIS119 3.5 11.4 1.0
O B:HOH338 3.7 20.9 1.0
OG1 B:THR199 3.9 12.8 1.0
OE1 B:GLU106 3.9 11.7 1.0
NE2 B:HIS119 4.0 12.8 1.0
CD2 B:HIS119 4.1 15.5 1.0
ND1 B:HIS94 4.1 14.4 1.0
O2 B:EVJ1 4.1 11.0 1.0
CG B:HIS94 4.1 16.0 1.0
CG B:HIS96 4.1 17.0 1.0
ND1 B:HIS96 4.2 12.7 1.0
C2 B:EVJ1 4.2 20.3 0.5
C2 B:EVJ1 4.2 14.1 0.5
CD B:GLU106 4.9 15.2 1.0
C3 B:EVJ1 4.9 20.4 0.5
CA B:HIS119 5.0 12.6 1.0
C3 B:EVJ1 5.0 18.4 0.5

Reference:

P.W.Snyder, J.Mecinovic, D.T.Moustakas, S.W.Thomas, M.Harder, E.T.Mack, M.R.Lockett, A.Heroux, W.Sherman, G.M.Whitesides. Mechanism of the Hydrophobic Effect in the Biomolecular Recognition of Arylsulfonamides By Carbonic Anhydrase. Proc.Natl.Acad.Sci.Usa V. 108 17889 2011.
ISSN: ISSN 0027-8424
PubMed: 22011572
DOI: 10.1073/PNAS.1114107108
Page generated: Sat Oct 26 15:35:33 2024

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