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Chlorine in PDB 2bws: HIS243ALA Escherichia Coli Aminopeptidase P

Enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P

All present enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P:
3.4.11.9;

Protein crystallography data

The structure of HIS243ALA Escherichia Coli Aminopeptidase P, PDB code: 2bws 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) 60.08 / 1.75
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 177.147, 177.147, 96.438, 90.00, 90.00, 120.00
R / Rfree (%) 15 / 16.5

Other elements in 2bws:

The structure of HIS243ALA Escherichia Coli Aminopeptidase P also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the HIS243ALA Escherichia Coli Aminopeptidase P (pdb code 2bws). 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 HIS243ALA Escherichia Coli Aminopeptidase P, PDB code: 2bws:

Chlorine binding site 1 out of 1 in 2bws

Go back to Chlorine Binding Sites List in 2bws
Chlorine binding site 1 out of 1 in the HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1443

b:23.6
occ:1.00
O A:HOH2230 3.2 33.0 1.0
O A:HOH2193 3.2 34.8 1.0
N A:VAL80 3.3 23.8 1.0
N A:SER111 3.3 23.0 1.0
O A:HOH2053 3.4 41.0 1.0
N A:PHE110 3.7 21.6 1.0
CB A:SER111 3.7 24.9 1.0
CA A:ARG79 3.8 22.7 1.0
CG1 A:VAL80 3.8 27.5 1.0
OG A:SER111 3.9 26.9 1.0
CB A:VAL80 3.9 25.8 1.0
C A:ARG79 4.1 21.0 1.0
CB A:ALA109 4.1 23.6 1.0
CB A:PHE110 4.1 21.4 1.0
CA A:SER111 4.1 25.2 1.0
O A:ASN78 4.1 21.4 1.0
CA A:PHE110 4.2 21.2 1.0
C A:PHE110 4.2 22.0 1.0
CA A:VAL80 4.2 24.3 1.0
C A:ALA109 4.3 21.3 1.0
CA A:ALA109 4.4 22.8 1.0
CB A:ARG79 4.6 23.3 1.0
N A:ARG79 4.7 22.0 1.0
C A:ASN78 4.8 22.9 1.0
CG A:ARG79 4.8 24.9 1.0
O A:HOH2144 5.0 44.9 1.0

Reference:

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
Page generated: Sat Dec 12 09:01:05 2020

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