Manganese in PDB 2bwt: ASP260ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of ASP260ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of ASP260ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwt 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)	23.89 / 2.90
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	137.588, 137.588, 231.948, 90.00, 90.00, 90.00
R / Rfree (%)	16.9 / 20.2

The structure of ASP260ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Manganese atom in the ASP260ALA Escherichia Coli Aminopeptidase P (pdb code 2bwt). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the ASP260ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwt:

Manganese binding site 1 out of 1 in the ASP260ALA 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 ASP260ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1441 b:56.2 occ:1.00 OD2 A:ASP271 2.1 63.7 1.0 OE2 A:GLU406 2.1 75.3 1.0 OE2 A:GLU383 2.2 80.5 1.0 NE2 A:HIS354 2.2 64.0 1.0 CD A:GLU406 2.9 73.0 1.0 OE1 A:GLU406 2.9 75.1 1.0 CD A:GLU383 3.0 75.7 1.0 CG A:ASP271 3.1 67.1 1.0 CD2 A:HIS354 3.2 65.1 1.0 CE1 A:HIS354 3.2 64.7 1.0 OE1 A:GLU383 3.2 78.4 1.0 OD1 A:ASP271 3.5 65.5 1.0 OG1 A:THR381 3.9 66.9 1.0 CG2 A:THR381 4.0 69.3 1.0 CB A:THR381 4.2 69.2 1.0 ND1 A:HIS354 4.3 64.8 1.0 CG A:HIS354 4.3 65.0 1.0 CG A:GLU406 4.3 71.8 1.0 CB A:ASP271 4.3 67.7 1.0 CG A:GLU383 4.4 74.6 1.0 C3 A:MPD1444 4.6 81.6 0.8 NE2 A:HIS361 4.8 71.4 1.0 CM A:MPD1444 4.8 81.5 0.8 O2 A:MPD1444 4.8 80.2 0.8 CB A:GLU383 4.9 73.3 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