Sodium in PDB 2bwu: ASP271ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of ASP271ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of ASP271ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwu 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)	22.65 / 2.20
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	138.589, 138.589, 232.056, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 19.3

The structure of ASP271ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Sodium atom in the ASP271ALA Escherichia Coli Aminopeptidase P (pdb code 2bwu). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the ASP271ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwu:

Sodium binding site 1 out of 1 in the ASP271ALA Escherichia Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of ASP271ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1441 b:51.0 occ:1.00 O A:HOH2137 2.1 62.5 1.0 OE2 A:GLU406 2.4 74.7 1.0 OE1 A:GLU383 2.5 87.4 1.0 NE2 A:HIS354 2.6 60.7 1.0 O A:HOH2105 2.8 60.1 1.0 CD A:GLU406 3.2 72.4 1.0 OE1 A:GLU406 3.3 73.1 1.0 CD A:GLU383 3.3 82.7 1.0 CE1 A:HIS354 3.5 63.0 1.0 CD2 A:HIS354 3.6 62.2 1.0 OE2 A:GLU383 3.7 87.8 1.0 CG2 A:THR381 4.3 62.9 1.0 OG1 A:THR381 4.3 64.5 1.0 O A:HOH2148 4.4 72.7 1.0 CB A:THR381 4.5 63.0 1.0 CG A:GLU383 4.5 73.3 1.0 NE2 A:HIS361 4.5 72.0 1.0 CB A:ALA271 4.6 64.1 1.0 CG A:GLU406 4.7 66.2 1.0 ND1 A:HIS354 4.7 58.3 1.0 CG A:HIS354 4.8 58.1 1.0 CB A:GLU383 4.9 66.9 1.0 OD2 A:ASP260 5.0 68.1 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