Manganese in PDB 2v3y: HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product

All present enzymatic activity of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product:
3.4.11.9;

The structure of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product, PDB code: 2v3y 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)	154.30 / 1.60
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.132, 177.132, 96.170, 90.00, 90.00, 120.00
R / Rfree (%)	15.4 / 16.7

The structure of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Manganese atom in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product (pdb code 2v3y). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product, PDB code: 2v3y:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:13.6 occ:1.00 O A:HOH2729 2.0 17.8 1.0 OE2 A:GLU406 2.1 12.6 1.0 NE2 A:HIS354 2.1 10.2 1.0 OD2 A:ASP271 2.1 11.1 1.0 OE2 A:GLU383 2.4 14.6 1.0 MN A:MN1442 3.0 13.6 1.0 CG A:ASP271 3.0 11.7 1.0 CD2 A:HIS354 3.1 8.4 1.0 CD A:GLU406 3.1 12.6 1.0 CD A:GLU383 3.1 11.8 1.0 CE1 A:HIS354 3.1 11.3 1.0 OE1 A:GLU383 3.2 14.7 1.0 OD1 A:ASP271 3.3 10.3 1.0 OE1 A:GLU406 3.4 12.4 1.0 CG2 A:THR381 3.8 9.5 1.0 OG1 A:THR381 3.8 8.8 1.0 CB A:THR381 4.0 9.0 1.0 ND1 A:HIS354 4.2 7.6 1.0 CG A:HIS354 4.2 8.5 1.0 CB A:ASP271 4.3 8.3 1.0 CG A:GLU406 4.4 7.1 1.0 CG A:GLU383 4.4 9.4 1.0 N B:PRO1 4.8 28.2 1.0 CB A:GLU383 4.9 9.8 1.0 CA B:PRO1 4.9 27.9 1.0

Manganese binding site 2 out of 2 in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:13.6 occ:1.00 O A:HOH2729 1.7 17.8 1.0 OD1 A:ASP271 2.0 10.3 1.0 OE1 A:GLU406 2.1 12.4 1.0 OD1 A:ASP260 2.2 8.9 1.0 OD2 A:ASP260 2.6 9.6 1.0 CG A:ASP260 2.7 9.8 1.0 CD A:GLU406 2.9 12.6 1.0 CG A:ASP271 2.9 11.7 1.0 MN A:MN1441 3.0 13.6 1.0 OE2 A:GLU406 3.1 12.6 1.0 OD2 A:ASP271 3.2 11.1 1.0 OG1 A:THR273 3.5 8.2 1.0 OH A:TYR229 3.8 8.7 1.0 OE1 A:GLU383 3.9 14.7 1.0 CB A:ASP260 4.2 7.8 1.0 CG A:GLU406 4.3 7.1 1.0 CZ A:TYR229 4.3 7.5 1.0 CB A:ASP271 4.3 8.3 1.0 C A:ASP271 4.5 7.8 1.0 CD A:GLU383 4.5 11.8 1.0 O A:ILE272 4.6 7.4 1.0 OE2 A:GLU383 4.6 14.6 1.0 O A:ASP271 4.6 7.7 1.0 C A:ILE272 4.7 7.5 1.0 N A:ILE272 4.7 5.5 1.0 CA A:ASP271 4.7 8.2 1.0 CE2 A:TYR229 4.7 9.3 1.0 CB A:GLU406 4.9 9.2 1.0 CB A:THR273 4.9 6.2 1.0 CA A:ASP260 4.9 8.3 1.0 NE A:ARG404 4.9 8.3 1.0 N A:THR273 4.9 8.5 1.0 CD B:PRO1 4.9 29.7 1.0 NE2 A:HIS354 5.0 10.2 1.0 N B:PRO1 5.0 28.2 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