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 / R_free (%)*	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: Fri Jul 11 00:39:37 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO

	© Copyright 2008-2020 by atomistry.com
Home \| Site Map \| Copyright \| Contact us \| Privacy