Manganese in PDB 2v3z: GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

All present enzymatic activity of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate:
3.4.11.9;

The structure of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3z was solved by S.C.Graham, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.66 / 1.56
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.695, 177.695, 96.433, 90.00, 90.00, 120.00
R / Rfree (%)	14 / 15

The structure of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate (pdb code 2v3z). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3z:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:17.7 occ:0.30 N B:VAL0 1.9 22.6 1.0 OD2 A:ASP271 2.1 11.6 1.0 NE2 A:HIS354 2.1 12.2 1.0 OE2 A:GLU406 2.5 14.3 1.0 O B:VAL0 2.8 20.9 1.0 O A:HOH2677 3.0 40.5 1.0 CG A:ASP271 3.0 12.0 1.0 CE1 A:HIS354 3.0 12.2 1.0 CA B:VAL0 3.0 23.7 1.0 MN A:MN1442 3.0 12.2 0.9 C B:VAL0 3.1 23.6 1.0 CD2 A:HIS354 3.1 11.8 1.0 OD1 A:ASP271 3.3 12.7 1.0 CD A:GLU406 3.4 14.9 1.0 CG1 B:VAL0 3.5 29.5 1.0 OE1 A:GLU406 3.7 14.6 1.0 CB B:VAL0 3.8 27.4 1.0 CG2 A:THR381 4.0 10.8 1.0 O A:HOH2663 4.0 31.6 1.0 N B:PRO1 4.1 19.2 1.0 ND1 A:HIS354 4.2 9.5 1.0 OG1 A:THR381 4.2 12.5 1.0 CG A:HIS354 4.2 8.5 1.0 CB A:ASP271 4.3 9.0 1.0 CB A:THR381 4.4 11.5 1.0 NE2 A:HIS361 4.6 12.9 1.0 CG2 A:VAL360 4.7 10.4 1.0 CG A:GLU406 4.8 10.6 1.0 CA B:PRO1 4.8 21.6 1.0 CD2 A:HIS361 4.8 11.0 1.0 O A:HOH2633 5.0 19.9 0.6

Manganese binding site 2 out of 2 in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:12.2 occ:0.90 N B:VAL0 1.8 22.6 1.0 OD1 A:ASP271 1.9 12.7 1.0 OE1 A:GLU406 2.0 14.6 1.0 OD1 A:ASP260 2.1 10.5 1.0 CG A:ASP260 2.7 10.3 1.0 OD2 A:ASP260 2.7 11.1 1.0 CD A:GLU406 2.9 14.9 1.0 CG A:ASP271 2.9 12.0 1.0 CA B:VAL0 2.9 23.7 1.0 MN A:MN1441 3.0 17.7 0.3 OE2 A:GLU406 3.1 14.3 1.0 OD2 A:ASP271 3.2 11.6 1.0 OG1 A:THR273 3.5 10.3 1.0 OH A:TYR229 3.6 11.1 1.0 CB B:VAL0 3.7 27.4 1.0 C B:VAL0 4.1 23.6 1.0 CG1 B:VAL0 4.1 29.5 1.0 O A:HOH2677 4.2 40.5 1.0 CB A:ASP260 4.2 8.6 1.0 CZ A:TYR229 4.2 9.9 1.0 CB A:ASP271 4.2 9.0 1.0 CG A:GLU406 4.2 10.6 1.0 C A:ASP271 4.4 9.7 1.0 O A:ILE272 4.4 8.1 1.0 C A:ILE272 4.5 8.4 1.0 N A:ILE272 4.5 8.1 1.0 CA A:ASP271 4.6 8.4 1.0 O A:ASP271 4.6 10.4 1.0 CE2 A:TYR229 4.6 11.1 1.0 O B:VAL0 4.6 20.9 1.0 N A:THR273 4.8 8.6 1.0 CA A:ASP260 4.8 8.3 1.0 CB A:GLU406 4.8 10.8 1.0 N B:PRO1 4.8 19.2 1.0 CB A:THR273 4.9 8.4 1.0 CE1 A:TYR229 4.9 9.3 1.0 CD B:PRO1 5.0 21.0 1.0 NE A:ARG404 5.0 9.1 1.0

S.C.Graham, J.M.Guss. Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu. Arch.Biochem.Biophys. V. 469 200 2008.
ISSN: ISSN 0003-9861
PubMed: 17983589
DOI: 10.1016/J.ABB.2007.10.009