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Chlorine in PDB 2v3z: GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

Enzymatic activity of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

All present enzymatic activity of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate:
3.4.11.9;

Protein crystallography data

The structure of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3z 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) 29.66 / 1.56
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 177.695, 177.695, 96.433, 90.00, 90.00, 120.00
R / Rfree (%) 14 / 15

Other elements in 2v3z:

The structure of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate (pdb code 2v3z). 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 GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3z:

Chlorine binding site 1 out of 1 in 2v3z

Go back to Chlorine Binding Sites List in 2v3z
Chlorine binding site 1 out of 1 in the GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of GLU383ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1443

b:24.3
occ:1.00
 O A:HOH2191 3.1 46.3 1.0
O A:HOH2297 3.2 32.8 1.0
O A:HOH2252 3.3 38.8 1.0
N A:VAL80 3.3 12.9 1.0
N A:SER111 3.4 12.6 1.0
CB A:SER111 3.7 16.2 1.0
N A:PHE110 3.7 11.6 1.0
CA A:ARG79 3.7 11.4 1.0
OG A:SER111 3.8 19.8 1.0
CG1 A:VAL80 3.9 15.4 1.0
CB A:VAL80 4.0 13.1 1.0
C A:ARG79 4.0 11.6 1.0
O A:ASN78 4.1 11.3 1.0
CA A:SER111 4.1 15.0 1.0
CB A:PHE110 4.1 13.2 1.0
CB A:ALA109 4.1 14.7 1.0
C A:PHE110 4.2 11.9 1.0
CA A:PHE110 4.2 11.7 1.0
CA A:VAL80 4.3 12.3 1.0
C A:ALA109 4.4 12.0 1.0
CA A:ALA109 4.5 12.9 1.0
CB A:ARG79 4.5 12.0 1.0
N A:ARG79 4.7 10.8 1.0
CG A:ARG79 4.7 13.9 1.0
C A:ASN78 4.8 10.9 1.0

Reference:

S.C.Graham, J.M.Guss. Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu. Arch.Biochem.Biophys. V. 469 200 2008.
ISSN: ISSN 0003-9861
PubMed: 17983589
DOI: 10.1016/J.ABB.2007.10.009
Page generated: Sat Jul 20 11:36:16 2024

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