Zinc in PDB 3qnv: Carboxypeptidase T

All present enzymatic activity of Carboxypeptidase T:
3.4.17.18;

The structure of Carboxypeptidase T, PDB code: 3qnv was solved by V.I.Timofeev, V.K.Akparov, I.P.Kuranova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.69
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	158.002, 158.002, 103.913, 90.00, 90.00, 120.00
R / Rfree (%)	16.9 / 18.2

The binding sites of Zinc atom in the Carboxypeptidase T (pdb code 3qnv). 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 Carboxypeptidase T, PDB code: 3qnv:

Zinc binding site 1 out of 1 in the Carboxypeptidase T


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase T within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:7.5 occ:1.00 O A:HOH339 2.0 10.8 1.0 ND1 A:HIS69 2.1 5.5 1.0 ND1 A:HIS204 2.1 5.7 1.0 OE1 A:GLU72 2.2 6.9 1.0 OE2 A:GLU72 2.4 6.7 1.0 CD A:GLU72 2.6 6.8 1.0 CE1 A:HIS69 3.0 5.6 1.0 CE1 A:HIS204 3.1 5.9 1.0 CG A:HIS204 3.1 5.7 1.0 CG A:HIS69 3.2 6.1 1.0 CB A:HIS204 3.4 5.5 1.0 CB A:HIS69 3.6 6.6 1.0 O A:HOH348 3.9 8.9 1.0 O A:THR205 4.0 6.2 1.0 O3 A:SO4405 4.1 12.8 1.0 O2 A:SO4405 4.1 12.7 1.0 CG A:GLU72 4.1 6.8 1.0 NE2 A:HIS69 4.1 5.7 1.0 NE2 A:HIS204 4.2 5.7 1.0 CD2 A:HIS204 4.2 5.6 1.0 CA A:HIS204 4.2 5.7 1.0 CD2 A:HIS69 4.3 5.8 1.0 O A:HOH335 4.4 14.4 1.0 N A:THR205 4.5 5.9 1.0 S A:SO4405 4.5 12.8 1.0 OE2 A:GLU277 4.5 12.9 1.0 NH1 A:ARG129 4.5 8.2 1.0 O1 A:SO4405 4.6 12.4 1.0 OE1 A:GLU277 4.8 11.9 1.0 N A:HIS69 4.8 7.0 1.0 CA A:HIS69 4.8 6.8 1.0 C A:HIS204 4.9 5.7 1.0 CB A:GLU72 4.9 6.8 1.0

V.K.Akparov, V.I.Timofeev, I.P.Kuranova. Three-Dimensional Structure of Recombinant Carboxypeptidase T From Thermoactinomyces Vulgaris Without Calcium Ions Crystallography Reports V. 56 596 2011.
ISSN: ISSN 1063-7745
DOI: 10.1134/S106377451104002X