Chlorine in PDB 2v3x: HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

Enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate

All present enzymatic activity of HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate:
3.4.11.9;

Protein crystallography data

The structure of HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate, PDB code: 2v3x 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)*	30.06 / 1.70
*Space group*	P 6₄ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	177.396, 177.396, 96.499, 90.00, 90.00, 120.00
*R / R_free (%)*	14.1 / 15.4

Other elements in 2v3x:

The structure of HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate (pdb code 2v3x). 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 in Complex with Substrate, PDB code: 2v3x:

Chlorine binding site 1 out of 1 in 2v3x

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Chlorine Binding Sites List in 2v3x

Chlorine binding site 1 out of 1 in the HIS243ALA 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 HIS243ALA Escherichia Coli Aminopeptidase P in Complex with Substrate within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1443 b:30.9 occ:1.00	O	A:HOH2249	3.2	42.4	1.0
	O	A:HOH2211	3.2	47.5	1.0
	N	A:VAL80	3.3	16.0	1.0
	N	A:SER111	3.4	15.6	1.0
	CB	A:SER111	3.7	19.1	1.0
	N	A:PHE110	3.7	14.7	1.0
	CA	A:ARG79	3.7	14.4	1.0
	OG	A:SER111	3.8	20.8	1.0
	CG1	A:VAL80	3.8	17.7	1.0
	CB	A:VAL80	4.0	16.8	1.0
	C	A:ARG79	4.0	13.5	1.0
	O	A:ASN78	4.1	13.6	1.0
	CA	A:SER111	4.1	17.4	1.0
	CB	A:ALA109	4.1	15.5	1.0
	CB	A:PHE110	4.1	15.0	1.0
	CA	A:PHE110	4.2	14.2	1.0
	C	A:PHE110	4.2	15.1	1.0
	CA	A:VAL80	4.3	16.2	1.0
	C	A:ALA109	4.4	13.2	1.0
	CA	A:ALA109	4.5	14.9	1.0
	CB	A:ARG79	4.5	14.9	1.0
	N	A:ARG79	4.7	14.3	1.0
	CG	A:ARG79	4.8	17.6	1.0
	C	A:ASN78	4.8	14.0	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 00:39:22 2025

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