Zinc in PDB 2boa: Human Procarboxypeptidase A4.

The structure of Human Procarboxypeptidase A4., PDB code: 2boa was solved by R.Garcia-Castellanos, R.Bonet-Figueredo, I.Pallares, S.Ventura, F.X.Aviles, J.Vendrell, F.X.Gomis-Ruth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.20
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	136.800, 87.200, 89.700, 90.00, 117.20, 90.00
R / Rfree (%)	22 / 29.3

The binding sites of Zinc atom in the Human Procarboxypeptidase A4. (pdb code 2boa). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Procarboxypeptidase A4., PDB code: 2boa:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Procarboxypeptidase A4.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Procarboxypeptidase A4. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1402 b:38.5 occ:0.87 OE2 A:GLU1072 2.0 32.5 1.0 OE1 A:GLU1072 2.0 35.0 1.0 O A:HOH1539 2.0 25.1 1.0 ND1 A:HIS1196 2.1 34.6 1.0 ND1 A:HIS1069 2.1 31.6 1.0 CD A:GLU1072 2.2 33.2 1.0 CE1 A:HIS1196 2.9 32.0 1.0 CG A:HIS1069 3.0 29.4 1.0 CE1 A:HIS1069 3.1 31.2 1.0 CG A:HIS1196 3.2 33.4 1.0 CB A:HIS1069 3.2 28.2 1.0 O A:HOH1559 3.6 13.2 1.0 CB A:HIS1196 3.6 32.4 1.0 CG A:GLU1072 3.7 30.4 1.0 NE2 A:HIS1196 4.1 32.6 1.0 O A:SER1197 4.1 32.3 1.0 CD2 A:HIS1069 4.2 29.6 1.0 O A:HOH1518 4.2 7.7 1.0 NE2 A:HIS1069 4.2 30.1 1.0 CD2 A:HIS1196 4.2 33.2 1.0 CA A:HIS1196 4.4 32.5 1.0 O A:HOH1517 4.4 27.0 1.0 CA A:HIS1069 4.5 28.7 1.0 N A:SER1197 4.6 31.8 1.0 N A:HIS1069 4.6 29.8 1.0 CB A:GLU1072 4.6 28.6 1.0 O A:HOH1620 4.6 27.7 1.0 CG2 A:ILE1068 4.9 31.5 1.0 NH2 A:ARG1127 4.9 30.7 1.0

Zinc binding site 2 out of 2 in the Human Procarboxypeptidase A4.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Procarboxypeptidase A4. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1403 b:36.2 occ:0.77 OE2 B:GLU1072 2.0 34.3 1.0 OE1 B:GLU1072 2.0 34.1 1.0 ND1 B:HIS1196 2.1 33.5 1.0 ND1 B:HIS1069 2.1 29.6 1.0 O B:HOH1536 2.1 47.7 1.0 CD B:GLU1072 2.2 31.9 1.0 CE1 B:HIS1196 3.0 31.3 1.0 CG B:HIS1069 3.0 27.6 1.0 CE1 B:HIS1069 3.1 27.0 1.0 CG B:HIS1196 3.1 31.7 1.0 CB B:HIS1069 3.3 27.0 1.0 CB B:HIS1196 3.5 30.6 1.0 CG B:GLU1072 3.7 29.7 1.0 O B:SER1197 4.0 31.6 1.0 NE2 B:HIS1196 4.1 32.7 1.0 O B:HOH1526 4.2 26.4 1.0 CD2 B:HIS1069 4.2 28.4 1.0 CD2 B:HIS1196 4.2 32.8 1.0 NE2 B:HIS1069 4.2 27.3 1.0 O B:HOH1605 4.2 30.9 1.0 CA B:HIS1196 4.2 30.5 1.0 N B:SER1197 4.4 31.1 1.0 CB B:GLU1072 4.6 28.4 1.0 CA B:HIS1069 4.6 27.4 1.0 OE2 B:GLU1270 4.7 48.1 1.0 N B:HIS1069 4.7 27.1 1.0 O B:HOH1632 4.7 32.5 1.0 CG2 B:ILE1068 4.8 28.0 1.0 C B:HIS1196 4.9 30.7 1.0 NH2 B:ARG1127 4.9 32.0 1.0 OE1 B:GLU1270 4.9 46.5 1.0

R.Garcia-Castellanos, R.Bonet-Figueredo, I.Pallares, S.Ventura, F.X.Aviles, J.Vendrell, F.X.Gomis-Ruth. Detailed Molecular Comparison Between the Inhibition Mode of A/B-Type Carboxypeptidases in the Zymogen State and By the Endogenous Inhibitor Latexin. Cell.Mol.Life Sci. V. 62 1996 2005.
ISSN: ISSN 1420-682X
PubMed: 16091843
DOI: 10.1007/S00018-005-5174-4