Zinc in PDB 3glj: A Polymorph of Carboxypeptidase B Zymogen Structure

All present enzymatic activity of A Polymorph of Carboxypeptidase B Zymogen Structure:
3.4.17.2;

The structure of A Polymorph of Carboxypeptidase B Zymogen Structure, PDB code: 3glj was solved by D.Fernandez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.63 / 1.89
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	49.590, 49.970, 50.630, 109.94, 104.50, 96.19
R / Rfree (%)	16.6 / 19.8

The binding sites of Zinc atom in the A Polymorph of Carboxypeptidase B Zymogen Structure (pdb code 3glj). 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 A Polymorph of Carboxypeptidase B Zymogen Structure, PDB code: 3glj:

Zinc binding site 1 out of 1 in the A Polymorph of Carboxypeptidase B Zymogen Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of A Polymorph of Carboxypeptidase B Zymogen Structure within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:21.1 occ:1.00 ND1 A:HIS69 2.1 12.3 1.0 ND1 A:HIS196 2.1 15.8 1.0 O A:HOH315 2.2 28.9 1.0 OE1 A:GLU72 2.2 10.1 1.0 OE2 A:GLU72 2.5 11.2 1.0 CD A:GLU72 2.7 11.2 1.0 CE1 A:HIS69 3.0 13.7 1.0 CG A:HIS196 3.1 12.5 1.0 CE1 A:HIS196 3.1 15.4 1.0 CG A:HIS69 3.2 11.0 1.0 CB A:HIS196 3.4 11.2 1.0 CB A:HIS69 3.6 9.4 1.0 O A:HOH408 3.8 13.9 1.0 NE2 A:HIS69 4.1 13.9 1.0 CG A:GLU72 4.2 10.4 1.0 NE2 A:HIS196 4.2 14.8 1.0 CD2 A:HIS196 4.2 13.6 1.0 CD2 A:HIS69 4.2 11.2 1.0 CA A:HIS196 4.3 10.8 1.0 O A:HOH329 4.4 33.1 1.0 O A:SER197 4.4 11.3 1.0 O A:HOH588 4.6 39.9 1.0 N A:SER197 4.7 10.9 1.0 N A:HIS69 4.7 9.4 1.0 CA A:HIS69 4.8 9.5 1.0 OE1 A:GLU270 4.9 24.4 1.0 CB A:GLU72 4.9 9.7 1.0 O A:HOH314 5.0 11.4 1.0

D.Fernandez, E.Boix, I.Pallares, F.X.Aviles, J.Vendrell. Analysis of A New Crystal Form of Procarboxypeptidase B: Further Insights Into the Catalytic Mechanism Biopolymers 2009.
ISSN: ESSN 1079-0282
PubMed: 19802820
DOI: 10.1002/BIP.21320