Chlorine in PDB 4asd: Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006)

Enzymatic activity of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006)

All present enzymatic activity of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006):
2.7.10.1;

Protein crystallography data

The structure of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006), PDB code: 4asd 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)*	15.00 / 2.03
*Space group*	C 1 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	135.818, 56.479, 52.052, 90.00, 95.42, 90.00
*R / R_free (%)*	17.5 / 23

Other elements in 4asd:

The structure of Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006) also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006) (pdb code 4asd). 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 Sorafenib (Bay 43-9006), PDB code: 4asd:

Chlorine binding site 1 out of 1 in 4asd

Go back to

Chlorine Binding Sites List in 4asd

Chlorine binding site 1 out of 1 in the Crystal Structure of VEGFR2 (Juxtamembrane and Kinase Domains) in Complex with Sorafenib (Bay 43-9006)

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 Sorafenib (Bay 43-9006) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1500 b:33.6 occ:1.00	CL11	A:BAX1500	0.0	33.6	1.0
	C5	A:BAX1500	1.7	29.0	1.0
	C4	A:BAX1500	2.7	28.4	1.0
	C6	A:BAX1500	2.7	27.9	1.0
	F9	A:BAX1500	3.1	29.6	1.0
	C7	A:BAX1500	3.1	28.4	1.0
	F8	A:BAX1500	3.1	28.9	1.0
	O	A:HOH2205	3.3	35.1	1.0
	O	A:HOH2054	3.6	47.1	1.0
	CD1	A:ILE892	3.9	23.9	1.0
	C3	A:BAX1500	4.0	27.7	1.0
	C1	A:BAX1500	4.0	28.1	1.0
	O	A:ILE1025	4.3	26.1	1.0
	F10	A:BAX1500	4.5	28.7	1.0
	CD2	A:LEU1019	4.5	24.5	1.0
	C2	A:BAX1500	4.5	26.8	1.0
	CD1	A:LEU1019	4.8	25.9	1.0
	CG2	A:ILE888	4.9	22.3	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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