Manganese in PDB 2bwy: GLU383ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of GLU383ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of GLU383ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwy 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)	119.52 / 2.40
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	138.578, 138.578, 231.389, 90.00, 90.00, 90.00
R / Rfree (%)	17.2 / 20.7

The structure of GLU383ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Manganese atom in the GLU383ALA Escherichia Coli Aminopeptidase P (pdb code 2bwy). 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, PDB code: 2bwy:
Jump to Manganese binding site number: 1; 2;

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:48.3 occ:1.00 OD2 A:ASP271 2.2 39.8 1.0 NE2 A:HIS354 2.2 41.1 1.0 OE2 A:GLU406 2.4 37.8 1.0 O A:HOH2187 2.7 25.7 1.0 MN A:MN1442 3.1 39.8 1.0 CG A:ASP271 3.1 37.3 1.0 CE1 A:HIS354 3.2 39.6 1.0 CD2 A:HIS354 3.3 40.6 1.0 CD A:GLU406 3.3 37.6 1.0 O4 A:SO41445 3.3 63.9 0.7 OD1 A:ASP271 3.4 41.0 1.0 OE1 A:GLU406 3.4 40.0 1.0 OG1 A:THR381 4.1 40.0 1.0 CG2 A:THR381 4.2 39.4 1.0 ND1 A:HIS354 4.3 39.7 1.0 CG A:HIS354 4.4 39.0 1.0 CB A:THR381 4.4 39.8 1.0 CB A:ASP271 4.4 36.6 1.0 S A:SO41445 4.6 66.3 0.7 NE2 A:HIS361 4.6 44.1 1.0 CG A:GLU406 4.7 36.7 1.0 O2 A:SO41445 4.7 65.2 0.7 CG2 A:VAL360 4.8 41.5 1.0 CD2 A:HIS361 4.8 43.6 1.0

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1442 b:39.8 occ:1.00 OE1 A:GLU406 2.1 40.0 1.0 OD1 A:ASP271 2.2 41.0 1.0 OD1 A:ASP260 2.2 35.5 1.0 OD2 A:ASP260 2.6 35.9 1.0 CG A:ASP260 2.7 38.8 1.0 CD A:GLU406 3.0 37.6 1.0 MN A:MN1441 3.1 48.3 1.0 CG A:ASP271 3.1 37.3 1.0 O A:HOH2187 3.2 25.7 1.0 OD2 A:ASP271 3.3 39.8 1.0 OE2 A:GLU406 3.4 37.8 1.0 OG1 A:THR273 3.5 33.1 1.0 OH A:TYR229 3.6 40.0 1.0 CZ A:TYR229 4.2 37.3 1.0 CB A:ASP260 4.2 38.0 1.0 CG A:GLU406 4.3 36.7 1.0 CB A:ASP271 4.4 36.6 1.0 O A:ILE272 4.5 32.1 1.0 O2 A:SO41445 4.5 65.2 0.7 CE2 A:TYR229 4.5 38.5 1.0 C A:ASP271 4.6 35.4 1.0 O4 A:SO41445 4.6 63.9 0.7 C A:ILE272 4.6 34.1 1.0 N A:ILE272 4.7 34.9 1.0 O A:ASP271 4.8 36.5 1.0 CA A:ASP271 4.8 36.0 1.0 NE A:ARG404 4.8 39.7 1.0 CB A:THR273 4.8 34.7 1.0 CB A:GLU406 4.9 37.9 1.0 N A:THR273 4.9 34.5 1.0 CE1 A:TYR229 4.9 36.8 1.0 CA A:ASP260 4.9 38.0 1.0

S.C.Graham, P.E.Lilley, M.Lee, P.M.Schaeffer, A.V.Kralicek, N.E.Dixon, J.M.Guss. Kinetic and Crystallographic Analysis of Mutant Escherichia Coli Aminopeptidase P: Insights Into Substrate Recognition and the Mechanism of Catalysis. Biochemistry V. 45 964 2006.
ISSN: ISSN 0006-2960
PubMed: 16411772
DOI: 10.1021/BI0518904