Chlorine in PDB 3ad5: Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)

Enzymatic activity of Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)

All present enzymatic activity of Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394):
2.7.10.2;

Protein crystallography data

The structure of Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 3ad5 was solved by E.Tsuji, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 2.00
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	41.961, 73.610, 91.960, 90.00, 90.00, 90.00
*R / R_free (%)*	15.4 / 21.8

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394) (pdb code 3ad5). 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 Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394), PDB code: 3ad5:

Chlorine binding site 1 out of 1 in 3ad5

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Chlorine Binding Sites List in 3ad5

Chlorine binding site 1 out of 1 in the Crystal Structure of Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394)

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 Triazolone Derivative Bound to the Kinase Domain of Human Lck, (Auto-Phosphorylated on TYR394) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1 b:0.4 occ:1.00	CL49	A:5PB1	0.0	0.4	1.0
	C42	A:5PB1	1.8	0.2	1.0
	O	A:HOH154	2.2	35.9	1.0
	C43	A:5PB1	2.8	0.5	1.0
	C41	A:5PB1	2.8	0.7	1.0
	O	A:HOH85	3.1	13.6	1.0
	O	A:HOH137	3.4	22.7	1.0
	O	A:HOH83	3.4	12.0	1.0
	CG2	A:THR316	3.8	5.3	1.0
	OG1	A:THR316	4.0	8.4	1.0
	NZ	A:LYS273	4.0	30.2	1.0
	C44	A:5PB1	4.1	0.9	1.0
	C40	A:5PB1	4.1	0.2	1.0
	OE2	A:GLU288	4.2	21.8	1.0
	CE	A:LYS273	4.3	24.2	1.0
	CB	A:THR316	4.5	8.6	1.0
	CD	A:LYS273	4.5	16.9	1.0
	C39	A:5PB1	4.6	0.5	1.0
	CD	A:GLU288	4.7	18.8	1.0
	OE1	A:GLU288	4.7	20.0	1.0
	CG2	A:ILE314	4.9	5.1	1.0
	CB	A:LYS273	5.0	8.9	1.0

Reference:

M.Ozawa, T.Ozawa, E.Tsuji, K.Okazaki, K.Takeda. Ab Initio Fragment Molecular Orbital Study of Ligand Binding to Leukocyte-Specific Protein Tyrosine (Lck) Kinase To Be Published.

Page generated: Sat Jul 20 15:50:11 2024

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