Manganese in PDB 2v3x: HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

All present enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate:
3.4.11.9;

The structure of HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3x 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)	30.06 / 1.70
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.396, 177.396, 96.499, 90.00, 90.00, 120.00
R / Rfree (%)	14.1 / 15.4

The structure of HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate (pdb code 2v3x). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3x:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:17.8 occ:0.80 OE2 A:GLU406 2.1 16.0 1.0 NE2 A:HIS354 2.2 13.9 1.0 OD2 A:ASP271 2.2 16.2 1.0 OE2 A:GLU383 2.3 24.4 1.0 MN A:MN1442 3.0 16.6 0.7 CD A:GLU383 3.0 22.8 1.0 CG A:ASP271 3.1 16.4 1.0 CD A:GLU406 3.1 18.3 1.0 CE1 A:HIS354 3.1 12.8 1.0 OE1 A:GLU383 3.2 29.2 1.0 CD2 A:HIS354 3.2 14.0 1.0 O B:VAL0 3.2 26.7 0.7 OD1 A:ASP271 3.3 16.7 1.0 OE1 A:GLU406 3.4 19.2 1.0 N B:VAL0 3.5 27.2 0.7 C B:VAL0 3.7 28.0 0.7 CG2 A:THR381 3.8 14.6 1.0 OG1 A:THR381 3.8 13.4 1.0 CB A:THR381 4.1 13.8 1.0 ND1 A:HIS354 4.2 11.5 1.0 CA B:VAL0 4.2 28.4 0.7 CG A:HIS354 4.3 10.5 1.0 CB A:ASP271 4.3 12.5 1.0 CG A:GLU406 4.4 13.6 1.0 N B:PRO1 4.4 29.6 0.7 CG A:GLU383 4.4 16.5 1.0 CA B:PRO1 4.6 28.9 0.7 NE2 A:HIS361 4.9 17.9 1.0 CB A:GLU383 4.9 15.7 1.0 CG2 A:VAL360 5.0 15.5 1.0

Manganese binding site 2 out of 2 in the HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:16.6 occ:0.70 OD1 A:ASP271 2.0 16.7 1.0 OE1 A:GLU406 2.1 19.2 1.0 OD1 A:ASP260 2.2 16.0 1.0 N B:VAL0 2.2 27.2 0.7 OD2 A:ASP260 2.5 16.5 1.0 CG A:ASP260 2.7 15.8 1.0 CG A:ASP271 3.0 16.4 1.0 CD A:GLU406 3.0 18.3 1.0 MN A:MN1441 3.0 17.8 0.8 OE2 A:GLU406 3.2 16.0 1.0 OD2 A:ASP271 3.2 16.2 1.0 CA B:VAL0 3.2 28.4 0.7 OG1 A:THR273 3.5 12.7 1.0 OH A:TYR229 3.7 14.8 1.0 C B:VAL0 3.8 28.0 0.7 OE1 A:GLU383 4.0 29.2 1.0 O B:VAL0 4.1 26.7 0.7 CB A:ASP260 4.2 13.8 1.0 CZ A:TYR229 4.3 14.0 1.0 CB A:ASP271 4.4 12.5 1.0 CG A:GLU406 4.4 13.6 1.0 N B:PRO1 4.4 29.6 0.7 CB B:VAL0 4.5 29.0 0.7 C A:ASP271 4.6 13.2 1.0 O A:ILE272 4.6 11.5 1.0 CD A:GLU383 4.7 22.8 1.0 CE2 A:TYR229 4.7 14.7 1.0 OE2 A:GLU383 4.7 24.4 1.0 C A:ILE272 4.7 11.8 1.0 N A:ILE272 4.7 10.4 1.0 CA A:ASP271 4.8 11.8 1.0 O A:ASP271 4.8 13.2 1.0 CD B:PRO1 4.8 29.4 0.7 NE A:ARG404 4.9 14.2 1.0 CA A:ASP260 4.9 12.1 1.0 CB A:THR273 4.9 10.8 1.0 CB A:GLU406 4.9 12.2 1.0 N A:THR273 5.0 10.8 1.0 CE1 A:TYR229 5.0 12.7 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