Zinc in PDB 1cnc: Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites

All present enzymatic activity of Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites:
4.2.1.1;

The structure of Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites, PDB code: 1cnc 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 / 2.20
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 Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites (pdb code 1cnc). 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 Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites, PDB code: 1cnc:

Zinc binding site 1 out of 1 in the Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Compensatory Plastic Effects in the Redesign of Protein-Zinc Binding Sites within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:14.4 occ:1.00 ND1 A:HIS119 2.1 9.7 1.0 O A:HOH263 2.2 14.2 1.0 NE2 A:HIS96 2.3 11.7 1.0 SG A:CYS94 2.3 14.3 1.0 CE1 A:HIS119 3.0 9.9 1.0 CD2 A:HIS96 3.0 11.5 1.0 CG A:HIS119 3.2 9.8 1.0 CE1 A:HIS96 3.4 11.9 1.0 CB A:CYS94 3.7 13.9 1.0 CB A:HIS119 3.7 9.8 1.0 O A:HOH352 4.0 22.8 1.0 NE2 A:HIS119 4.1 10.1 1.0 OG1 A:THR199 4.2 9.2 1.0 O A:CYS94 4.2 12.8 1.0 CG A:HIS96 4.2 11.7 1.0 CD2 A:HIS119 4.3 10.0 1.0 OE1 A:GLU106 4.3 10.1 1.0 C A:CYS94 4.4 13.1 1.0 ND1 A:HIS96 4.4 11.7 1.0 O A:HOH264 4.4 21.7 1.0 CA A:CYS94 4.6 13.7 1.0 CA A:HIS119 4.8 9.9 1.0 N A:PHE95 4.9 12.8 1.0 N A:HIS119 5.0 10.0 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