Chlorine in PDB 2v3y: HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product

Enzymatic activity of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product

All present enzymatic activity of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product:
3.4.11.9;

Protein crystallography data

The structure of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product, PDB code: 2v3y 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 / 1.60
*Space group*	P 6₄ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	177.132, 177.132, 96.170, 90.00, 90.00, 120.00
*R / R_free (%)*	15.4 / 16.7

Other elements in 2v3y:

The structure of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product (pdb code 2v3y). 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 HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product, PDB code: 2v3y:

Chlorine binding site 1 out of 1 in 2v3y

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Chlorine Binding Sites List in 2v3y

Chlorine binding site 1 out of 1 in the HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of HIS361ALA Escherichia Coli Aminopeptidase P in Complex with Product within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1443 b:23.8 occ:1.00	O	A:HOH2299	3.2	33.2	1.0
	O	A:HOH2190	3.2	42.4	1.0
	N	A:VAL80	3.3	12.6	1.0
	O	A:HOH2256	3.3	32.8	1.0
	N	A:SER111	3.3	11.2	1.0
	CG1	A:VAL80	3.6	7.8	0.2
	CB	A:SER111	3.7	15.4	1.0
	CA	A:ARG79	3.7	10.9	0.3
	CA	A:ARG79	3.7	12.6	0.7
	CG2	A:VAL80	3.7	11.4	0.2
	N	A:PHE110	3.8	10.8	1.0
	OG	A:SER111	3.8	17.6	1.0
	CG1	A:VAL80	4.0	13.1	0.8
	CB	A:VAL80	4.0	11.9	0.8
	C	A:ARG79	4.0	11.4	1.0
	CB	A:VAL80	4.0	12.0	0.2
	O	A:ASN78	4.1	10.8	1.0
	CA	A:SER111	4.1	13.9	1.0
	CB	A:PHE110	4.1	12.1	1.0
	CB	A:ALA109	4.2	13.3	1.0
	C	A:PHE110	4.2	10.9	1.0
	CA	A:PHE110	4.2	11.9	1.0
	CA	A:VAL80	4.3	12.3	0.8
	CA	A:VAL80	4.3	12.0	0.2
	C	A:ALA109	4.4	11.3	1.0
	CB	A:ARG79	4.5	10.6	0.3
	CB	A:ARG79	4.5	12.7	0.7
	CA	A:ALA109	4.5	12.2	1.0
	CG	A:ARG79	4.6	8.5	0.3
	N	A:ARG79	4.7	11.9	1.0
	C	A:ASN78	4.7	10.9	1.0
	CG	A:ARG79	4.7	15.1	0.7

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 11:36:15 2024

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