Zinc in PDB 1yme: Structure of Carboxypeptidase

All present enzymatic activity of Structure of Carboxypeptidase:
3.4.17.1;

The structure of Structure of Carboxypeptidase, PDB code: 1yme was solved by H.M.Greenblatt, P.A.Tucker, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.53
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	51.620, 60.170, 47.170, 90.00, 97.40, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Structure of Carboxypeptidase (pdb code 1yme). 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 Structure of Carboxypeptidase, PDB code: 1yme:

Zinc binding site 1 out of 1 in the Structure of Carboxypeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Carboxypeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn310 b:14.3 occ:1.00 ND1 A:HIS69 1.9 10.5 1.0 O A:HOH416 1.9 13.7 1.0 ND1 A:HIS196 2.1 10.3 1.0 OE1 A:GLU72 2.2 12.9 1.0 OE2 A:GLU72 2.3 11.8 1.0 CD A:GLU72 2.6 12.7 1.0 CE1 A:HIS69 2.9 13.4 1.0 CG A:HIS69 3.0 9.5 1.0 CE1 A:HIS196 3.1 15.7 1.0 CG A:HIS196 3.1 10.8 1.0 CB A:HIS69 3.3 12.3 1.0 CB A:HIS196 3.4 11.1 1.0 O A:HOH482 3.7 39.8 1.0 O A:SER197 4.0 10.1 1.0 O A:HOH527 4.0 43.0 1.0 O A:HOH407 4.1 10.4 0.8 CG A:GLU72 4.1 13.3 1.0 NE2 A:HIS69 4.1 13.2 1.0 OE2 A:GLU270 4.1 16.5 1.0 CD2 A:HIS69 4.1 9.5 1.0 CA A:HIS196 4.2 8.4 1.0 NE2 A:HIS196 4.2 13.6 1.0 CD2 A:HIS196 4.2 13.4 1.0 N A:SER197 4.3 9.3 1.0 O A:HOH453 4.3 22.9 1.0 OE1 A:GLU270 4.6 17.1 1.0 CA A:HIS69 4.7 8.7 1.0 NH2 A:ARG127 4.8 25.9 1.0 CD A:GLU270 4.8 15.9 1.0 C A:HIS196 4.8 10.0 1.0 O A:HOH537 4.8 35.4 1.0 N A:HIS69 4.9 9.8 1.0 CB A:GLU72 4.9 10.4 1.0 C A:SER197 5.0 11.9 1.0

H.M.Greenblatt, H.Feinberg, P.A.Tucker, G.Shoham. Carboxypeptidase A: Native, Zinc-Removed and Mercury-Replaced Forms. Acta Crystallogr.,Sect.D V. 54 289 1998.
ISSN: ISSN 0907-4449
PubMed: 9867434
DOI: 10.1107/S0907444997010445