Chlorine in PDB 3o8t: Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding

Enzymatic activity of Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding

All present enzymatic activity of Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding:
2.7.11.24;

Protein crystallography data

The structure of Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding, PDB code: 3o8t was solved by H.V.Namboodiri, M.Karpusas, M.Bukhtiyarova, E.B.Springman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	37.84 / 2.00
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	68.489, 70.724, 75.682, 90.00, 90.00, 90.00
*R / R_free (%)*	22.5 / 28.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding (pdb code 3o8t). 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 Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding, PDB code: 3o8t:

Chlorine binding site 1 out of 1 in 3o8t

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Chlorine Binding Sites List in 3o8t

Chlorine binding site 1 out of 1 in the Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Conformational Plasticity of P38 Map Kinase Dfg-Motif Mutants in Response to Inhibitor Binding within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl361 b:35.6 occ:1.00	CL6	A:BMU361	0.0	35.6	1.0
	C6	A:BMU361	1.8	33.7	1.0
	C7	A:BMU361	2.8	34.0	1.0
	C5	A:BMU361	2.8	32.2	1.0
	CB	A:ALA51	3.9	30.2	1.0
	CG1	A:VAL38	3.9	37.8	1.0
	CG2	A:THR106	4.0	28.7	1.0
	C8	A:BMU361	4.1	33.1	1.0
	C4	A:BMU361	4.1	32.2	1.0
	CG2	A:VAL38	4.1	37.1	1.0
	CB	A:LYS53	4.3	29.7	1.0
	C3	A:BMU361	4.6	31.8	1.0
	CB	A:VAL38	4.7	37.1	1.0
	C	A:ALA51	4.9	29.7	1.0
	O	A:ALA51	4.9	29.7	1.0
	CG	A:LYS53	4.9	31.0	1.0
	N	A:LYS53	4.9	29.7	1.0

Reference:

H.V.Namboodiri, E.B.Springman, M.Karpusas, M.Bukhtiyarova, J.Ramcharan. Conformational Plasticity of P38 Map Kinase Dfg Motif Mutants in Response to Inhibitor Binding To Be Published.

Page generated: Sun Jul 21 01:28:07 2024

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