Zinc in PDB 1cve: Structural Consequences of Redesigning A Protein-Zinc Binding Site

All present enzymatic activity of Structural Consequences of Redesigning A Protein-Zinc Binding Site:
4.2.1.1;

The structure of Structural Consequences of Redesigning A Protein-Zinc Binding Site, PDB code: 1cve was solved by J.A.Ippolito, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 2.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Structural Consequences of Redesigning A Protein-Zinc Binding Site (pdb code 1cve). 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 Structural Consequences of Redesigning A Protein-Zinc Binding Site, PDB code: 1cve:

Zinc binding site 1 out of 1 in the Structural Consequences of Redesigning A Protein-Zinc Binding Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Consequences of Redesigning A Protein-Zinc Binding Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:16.7 occ:1.00 NE2 A:HIS96 2.0 9.3 1.0 NE2 A:HIS94 2.2 8.2 1.0 O A:HOH263 2.2 23.1 1.0 O A:HOH264 2.4 15.9 1.0 OD2 A:ASP119 2.8 11.7 1.0 CE1 A:HIS96 2.9 9.4 1.0 CD2 A:HIS96 3.0 9.2 1.0 CD2 A:HIS94 3.1 8.2 1.0 CE1 A:HIS94 3.2 8.2 1.0 OG1 A:THR199 3.4 5.9 1.0 O A:HOH342 3.6 17.0 1.0 O A:HOH350 3.7 20.8 1.0 OE1 A:GLU106 3.8 9.2 1.0 CG A:ASP119 3.9 11.4 1.0 O A:HOH353 4.1 18.5 1.0 ND1 A:HIS96 4.1 9.5 1.0 CG A:HIS96 4.1 9.4 1.0 CB A:ASP119 4.2 10.9 1.0 O A:HOH382 4.3 31.2 1.0 CG A:HIS94 4.3 8.1 1.0 ND1 A:HIS94 4.3 8.2 1.0 CD A:GLU106 4.6 9.7 1.0 O A:HOH351 4.7 33.8 1.0 CB A:THR199 4.8 6.2 1.0 OD1 A:ASP119 4.9 12.1 1.0

J.A.Ippolito, D.W.Christianson. Structural Consequences of Redesigning A Protein-Zinc Binding Site. Biochemistry V. 33 15241 1994.
ISSN: ISSN 0006-2960
PubMed: 7803386
DOI: 10.1021/BI00255A004