Chlorine in PDB 2bwx: HIS354ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of HIS354ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

The structure of HIS354ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwx 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)	154.30 / 1.70
Space group	P 64 2 2
Cell size a, b, c (Å), α, β, γ (°)	177.252, 177.252, 96.770, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / 17.6

The structure of HIS354ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Chlorine atom in the HIS354ALA Escherichia Coli Aminopeptidase P (pdb code 2bwx). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the HIS354ALA Escherichia Coli Aminopeptidase P, PDB code: 2bwx:

Chlorine binding site 1 out of 1 in the HIS354ALA Escherichia Coli Aminopeptidase P


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HIS354ALA Escherichia Coli Aminopeptidase P within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1442 b:30.3 occ:1.00 O A:HOH2233 3.1 38.4 1.0 N A:VAL80 3.3 21.2 1.0 N A:SER111 3.3 18.6 1.0 O A:HOH2143 3.4 49.7 1.0 CB A:SER111 3.6 20.9 1.0 N A:PHE110 3.7 17.6 1.0 CA A:ARG79 3.7 19.8 1.0 OG A:SER111 3.8 23.5 1.0 CG1 A:VAL80 3.8 26.4 1.0 CB A:VAL80 3.9 22.2 1.0 C A:ARG79 4.0 19.2 1.0 CA A:SER111 4.1 20.8 1.0 CB A:PHE110 4.1 17.9 1.0 CB A:ALA109 4.1 18.9 1.0 O A:ASN78 4.1 17.7 1.0 CA A:PHE110 4.2 17.5 1.0 C A:PHE110 4.2 18.3 1.0 CA A:VAL80 4.2 21.6 1.0 C A:ALA109 4.3 17.5 1.0 CA A:ALA109 4.4 18.1 1.0 CB A:ARG79 4.5 21.3 1.0 N A:ARG79 4.7 18.9 1.0 C A:ASN78 4.8 19.0 1.0 CG A:ARG79 4.8 20.8 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