Chlorine in PDB 4ase: Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951)

Enzymatic activity of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951)

All present enzymatic activity of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951):
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951), PDB code: 4ase was solved by M.Mctigue, Y.Deng, K.Ryan, A.Brooun, W.Diehl, A.Stewart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	43.32 / 1.83
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	135.095, 56.299, 51.991, 90.00, 96.33, 90.00
*R / R_free (%)*	20.7 / 23.1

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951) (pdb code 4ase). 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 Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951), PDB code: 4ase:

Chlorine binding site 1 out of 1 in 4ase

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Chlorine Binding Sites List in 4ase

Chlorine binding site 1 out of 1 in the Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951)

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Tivozanib (Av-951) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl3169 b:35.8 occ:1.00	CL4	A:AV93169	0.0	35.8	1.0
	C11	A:AV93169	1.7	25.0	1.0
	C13	A:AV93169	2.7	26.1	1.0
	C15	A:AV93169	2.8	27.8	1.0
	N28	A:AV93169	3.0	27.1	1.0
	CB	A:LYS868	3.5	25.8	1.0
	CG1	A:VAL916	3.5	23.3	1.0
	CG2	A:VAL916	3.8	22.7	1.0
	CD	A:LYS868	3.9	34.4	1.0
	O	A:VAL914	4.0	22.8	1.0
	C12	A:AV93169	4.1	24.5	1.0
	C16	A:AV93169	4.1	27.9	1.0
	CG1	A:VAL914	4.1	23.4	1.0
	OE2	A:GLU885	4.2	41.3	1.0
	C35	A:AV93169	4.2	30.0	1.0
	CB	A:VAL916	4.3	23.9	1.0
	CG	A:LYS868	4.3	29.9	1.0
	N	A:LYS868	4.4	25.1	1.0
	CB	A:VAL914	4.5	22.8	1.0
	CA	A:LYS868	4.5	25.9	1.0
	C17	A:AV93169	4.6	27.7	1.0
	C	A:VAL914	4.7	22.9	1.0
	N37	A:AV93169	4.9	31.0	1.0
	O36	A:AV93169	4.9	27.1	1.0

Reference:

M.Mctigue, B.W.Murray, J.H.Chen, Y.Deng, J.Solowiej, R.S.Kania. Molecular Conformations, Interactions, and Properties Associated with Drug Efficiency and Clinical Performance Among Vegfr Tk Inhibitors. Proc.Natl.Acad.Sci.Usa V. 109 18281 2012.
ISSN: ISSN 0027-8424
PubMed: 22988103
DOI: 10.1073/PNAS.1207759109

Page generated: Sat Dec 12 10:24:28 2020

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