Zinc in PDB 6i6z: Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh

All present enzymatic activity of Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh:
3.4.17.1;

The structure of Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh, PDB code: 6i6z was solved by P.Gallego, D.Reverter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.44 / 1.72
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	46.121, 84.109, 158.195, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 18.3

The binding sites of Zinc atom in the Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh (pdb code 6i6z). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh, PDB code: 6i6z:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:8.6 occ:1.00 O4 A:TJE501 1.9 12.9 1.0 OE1 A:GLU182 2.0 7.7 1.0 ND1 A:HIS306 2.0 8.3 1.0 ND1 A:HIS179 2.1 7.5 1.0 CD A:GLU182 2.7 8.2 1.0 OE2 A:GLU182 2.8 9.2 1.0 CE1 A:HIS306 2.9 13.2 1.0 CE1 A:HIS179 3.0 7.7 1.0 P1 A:TJE501 3.0 13.0 1.0 O7 A:TJE501 3.1 15.6 1.0 CG A:HIS179 3.1 7.6 1.0 CG A:HIS306 3.1 7.8 1.0 CB A:HIS179 3.5 6.2 1.0 CB A:HIS306 3.5 5.2 1.0 O A:HOH653 3.9 11.2 1.0 NE2 A:HIS306 4.1 13.5 1.0 C12 A:TJE501 4.1 11.7 1.0 NE2 A:HIS179 4.1 7.2 1.0 CD2 A:HIS306 4.2 12.9 1.0 CG A:GLU182 4.2 5.6 1.0 CD2 A:HIS179 4.2 7.2 1.0 O A:SER307 4.2 8.3 1.0 O A:HOH657 4.3 11.9 1.0 OE1 A:GLU380 4.4 14.6 1.0 C14 A:TJE501 4.4 9.2 1.0 NH2 A:ARG237 4.5 9.4 1.0 CA A:HIS306 4.5 4.5 1.0 C15 A:TJE501 4.6 11.0 1.0 CA A:HIS179 4.8 6.2 1.0 O6 A:TJE501 4.8 12.9 1.0 N A:SER307 4.8 4.7 1.0 OE2 A:GLU380 4.9 9.9 1.0 C13 A:TJE501 4.9 14.1 1.0 N A:HIS179 4.9 9.1 1.0 C24 A:TJE501 5.0 11.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Human Carboxypeptidase A1 in Complex with the Phosphinic Inhibitor Acetyl-Tyr-Ala-Y(PO2CH2)-Homophe-Oh within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn502 b:8.7 occ:1.00 O4 B:TJE501 2.0 12.7 1.0 ND1 B:HIS306 2.0 8.4 1.0 OE1 B:GLU182 2.0 8.4 1.0 ND1 B:HIS179 2.1 8.7 1.0 CD B:GLU182 2.7 8.6 1.0 OE2 B:GLU182 2.7 9.6 1.0 CE1 B:HIS306 2.9 12.9 1.0 P1 B:TJE501 3.0 11.6 1.0 CE1 B:HIS179 3.1 9.0 1.0 CG B:HIS306 3.1 8.7 1.0 CG B:HIS179 3.1 8.4 1.0 O7 B:TJE501 3.1 12.7 1.0 CB B:HIS179 3.4 7.9 1.0 CB B:HIS306 3.5 7.9 1.0 O B:HOH633 4.0 9.9 1.0 NE2 B:HIS306 4.1 14.6 1.0 C12 B:TJE501 4.1 13.2 1.0 CD2 B:HIS306 4.2 11.7 1.0 NE2 B:HIS179 4.2 6.7 1.0 CG B:GLU182 4.2 4.7 1.0 O B:HOH625 4.2 14.1 1.0 O B:SER307 4.2 8.2 1.0 CD2 B:HIS179 4.2 6.5 1.0 OE1 B:GLU380 4.3 12.1 1.0 C14 B:TJE501 4.4 11.9 1.0 CA B:HIS306 4.5 7.0 1.0 NH2 B:ARG237 4.6 9.0 1.0 C15 B:TJE501 4.7 14.4 1.0 N B:SER307 4.7 6.1 1.0 CA B:HIS179 4.8 5.6 1.0 OE2 B:GLU380 4.8 12.3 1.0 O6 B:TJE501 4.9 15.7 1.0 C13 B:TJE501 4.9 14.0 1.0 N B:HIS179 4.9 6.9 1.0

G.Covaleda, P.Gallego, J.Vendrell, D.Georgiadis, J.Lorenzo, V.Dive, F.X.Aviles, D.Reverter, L.Devel. Synthesis and Structural/Functional Characterization of Selective M14 Metallocarboxypeptidase Inhibitors Based on Phosphinic Pseudopeptide Scaffold: Implications on the Design of Specific Optical Probes. J. Med. Chem. V. 62 1917 2019.
ISSN: ISSN 1520-4804
PubMed: 30688452
DOI: 10.1021/ACS.JMEDCHEM.8B01465