Zinc in PDB 1aye: Human Procarboxypeptidase A2

All present enzymatic activity of Human Procarboxypeptidase A2:
3.4.17.15;

The structure of Human Procarboxypeptidase A2, PDB code: 1aye was solved by I.Garcia-Saez, D.Reverte, J.Vendrell, F.X.Aviles, M.Coll, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.200, 87.070, 59.020, 90.00, 99.35, 90.00
R / Rfree (%)	17.8 / 22.2

The binding sites of Zinc atom in the Human Procarboxypeptidase A2 (pdb code 1aye). 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 Human Procarboxypeptidase A2, PDB code: 1aye:

Zinc binding site 1 out of 1 in the Human Procarboxypeptidase A2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Procarboxypeptidase A2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:17.1 occ:1.00 O A:HOH401 2.0 18.5 1.0 OE1 A:GLU72 2.1 12.5 1.0 OE2 A:GLU72 2.1 13.2 1.0 ND1 A:HIS69 2.1 12.6 1.0 ND1 A:HIS196 2.1 12.0 1.0 CD A:GLU72 2.4 13.0 1.0 CE1 A:HIS69 3.0 12.2 1.0 CG A:HIS196 3.1 11.0 1.0 CE1 A:HIS196 3.1 12.5 1.0 CG A:HIS69 3.1 13.1 1.0 CB A:HIS196 3.4 9.3 1.0 CB A:HIS69 3.5 11.1 1.0 CG A:GLU72 4.0 11.3 1.0 O A:HOH564 4.0 34.8 1.0 O A:HOH410 4.1 12.0 1.0 O A:HOH447 4.1 36.3 1.0 OE2 A:GLU270 4.1 15.4 1.0 O A:SER197 4.1 14.2 1.0 NE2 A:HIS69 4.2 11.7 1.0 NE2 A:HIS196 4.2 16.3 1.0 CD2 A:HIS196 4.2 12.2 1.0 CA A:HIS196 4.2 10.8 1.0 CD2 A:HIS69 4.2 10.1 1.0 N A:SER197 4.5 11.0 1.0 O A:HOH450 4.7 13.6 1.0 NH2 A:ARG127 4.8 25.0 1.0 OE1 A:GLU270 4.8 17.6 1.0 CA A:HIS69 4.8 12.7 1.0 CD A:GLU270 4.9 16.6 1.0 O A:HOH471 4.9 35.2 1.0 CB A:GLU72 4.9 9.0 1.0 C A:HIS196 4.9 11.8 1.0 N A:HIS69 5.0 12.2 1.0

I.Garcia-Saez, D.Reverter, J.Vendrell, F.X.Aviles, M.Coll. The Three-Dimensional Structure of Human Procarboxypeptidase A2. Deciphering the Basis of the Inhibition, Activation and Intrinsic Activity of the Zymogen. Embo J. V. 16 6906 1997.
ISSN: ISSN 0261-4189
PubMed: 9384570
DOI: 10.1093/EMBOJ/16.23.6906