Magnesium 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:

Manganese

(Mn)

2 atoms

The binding sites of Magnesium atom in the GLU383ALA Escherichia Coli Aminopeptidase P (pdb code 2bwy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the GLU383ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwy:

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of GLU383ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1443 b:43.1 occ:1.00 O A:HOH2167 2.2 44.0 1.0 O A:HOH2169 2.2 43.2 1.0 O A:HOH2170 2.2 46.2 1.0 O A:ARG399 3.8 34.5 1.0 OE2 A:GLU396 3.9 39.4 1.0 O A:GLN397 4.3 35.1 1.0 O A:HOH2137 4.5 41.4 1.0 O A:GLU396 4.6 34.9 1.0 C A:GLN397 4.8 34.3 1.0 CD A:GLU396 4.8 36.5 1.0 O A:HOH2110 4.8 42.6 1.0 O A:HOH2171 4.9 39.7 1.0 CA A:GLN397 4.9 34.2 1.0 C A:ARG399 5.0 34.4 1.0 OE1 A:GLU396 5.0 37.8 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