Zinc in PDB 4a37: Metallo-Carboxypeptidase From Pseudomonas Aeruginosa

The structure of Metallo-Carboxypeptidase From Pseudomonas Aeruginosa, PDB code: 4a37 was solved by A.Otero, M.Rodriguez De La Vega, S.M.Tanco, J.Lorenzo, F.X.Aviles, D.Reverter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.76 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.890, 83.840, 107.450, 90.00, 96.37, 90.00
R / Rfree (%)	19.8 / 21.3

The binding sites of Zinc atom in the Metallo-Carboxypeptidase From Pseudomonas Aeruginosa (pdb code 4a37). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Metallo-Carboxypeptidase From Pseudomonas Aeruginosa, PDB code: 4a37:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Metallo-Carboxypeptidase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Metallo-Carboxypeptidase From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn376 b:15.7 occ:1.00 ND1 A:HIS167 2.1 10.6 1.0 ND1 A:HIS260 2.1 8.3 1.0 O A:HOH2177 2.1 14.2 1.0 OE1 A:GLU170 2.2 6.3 1.0 OE2 A:GLU170 2.5 10.5 1.0 CD A:GLU170 2.7 9.2 1.0 CE1 A:HIS167 3.0 9.9 1.0 CE1 A:HIS260 3.0 7.0 1.0 CG A:HIS260 3.1 6.8 1.0 CG A:HIS167 3.1 9.1 1.0 CB A:HIS260 3.4 6.6 1.0 CB A:HIS167 3.5 10.2 1.0 O A:HOH2175 3.6 12.0 1.0 O A:GLY261 4.1 8.6 1.0 NE2 A:HIS167 4.1 9.6 1.0 O A:HOH2179 4.1 22.1 1.0 CG A:GLU170 4.2 9.3 1.0 NE2 A:HIS260 4.2 7.5 1.0 CD2 A:HIS167 4.2 9.9 1.0 CD2 A:HIS260 4.2 8.4 1.0 NH1 A:ARG218 4.3 23.2 1.0 CA A:HIS260 4.3 6.0 1.0 N A:GLY261 4.3 8.2 1.0 O A:HOH2201 4.7 22.8 1.0 CA A:HIS167 4.8 7.8 1.0 O A:HOH2178 4.8 16.4 1.0 N A:HIS167 4.8 9.9 1.0 OE2 A:GLU335 4.8 25.4 1.0 OE1 A:GLU335 4.8 21.1 1.0 CB A:GLU170 4.9 8.6 1.0 C A:HIS260 4.9 6.0 1.0

Zinc binding site 2 out of 2 in the Metallo-Carboxypeptidase From Pseudomonas Aeruginosa


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Metallo-Carboxypeptidase From Pseudomonas Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn753 b:21.1 occ:1.00 ND1 B:HIS167 2.1 13.5 1.0 ND1 B:HIS260 2.1 13.7 1.0 O B:HOH2154 2.1 18.3 1.0 OE1 B:GLU170 2.1 14.7 1.0 OE2 B:GLU170 2.4 16.4 1.0 CD B:GLU170 2.6 14.8 1.0 CE1 B:HIS167 3.0 13.9 1.0 CE1 B:HIS260 3.0 14.4 1.0 CG B:HIS167 3.1 13.3 1.0 CG B:HIS260 3.1 13.8 1.0 O B:HOH2152 3.4 14.9 1.0 CB B:HIS260 3.5 13.6 1.0 CB B:HIS167 3.5 12.4 1.0 O B:HOH2157 3.9 28.1 1.0 O B:GLY261 4.0 15.8 1.0 CG B:GLU170 4.1 14.1 1.0 NE2 B:HIS167 4.1 12.8 1.0 NE2 B:HIS260 4.2 15.2 1.0 CD2 B:HIS167 4.2 12.2 1.0 CD2 B:HIS260 4.2 15.0 1.0 CA B:HIS260 4.3 13.1 1.0 N B:GLY261 4.3 14.2 1.0 NH1 B:ARG218 4.5 22.9 1.0 CA B:HIS167 4.8 11.8 1.0 N B:HIS167 4.8 12.4 1.0 CB B:GLU170 4.8 11.5 1.0 C B:HIS260 4.9 12.3 1.0 O B:HOH2156 4.9 18.0 1.0 OE1 B:GLU335 4.9 29.1 1.0

A.Otero, M.Rodriguez De La Vega, S.M.Tanco, J.Lorenzo, F.X.Aviles, D.Reverter. The Novel Structure of A Cytosolic M14 Metallocarboxypeptidase (Ccp) From Pseudomonas Aeruginosa: A Model For Mammalian Ccps. Faseb J. V. 26 3754 2012.
ISSN: ISSN 0892-6638
PubMed: 22645247
DOI: 10.1096/FJ.12-209601