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Conformational plasticity of P38 MAP kinase dfg motif mutants in response to inhibitor binding

Analyse Conformational plasticity of P38 MAP kinase dfg motif mutants in response to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OC1
Type: protein
Length: 330 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 14
EC: 2.7.11.24
UniProt: Q16539
Ligands: BMU
Pockets: 6 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	330	38% helix, 12% strand	Q16539

Ligands and binding sites

BMU · 1-(5-tert-butyl-2-methyl-2H-pyrazol-3-yl)-3-(4-chloro-phenyl)-urea · ligand · chains A
EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	504	0.69	0.79	55	BMU, EDO
2	104	0.60	0.86	23	empty
3	127	0.43	0.76	17	empty
4	67	0.31	0.75	18	empty
5	64	0.29	0.74	16	empty

Compared structures

3OC1 · Conformational plasticity of p38 MAP kinase DFG motif mutants in response to inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q16539
Elsewhere: RCSB PDB 3OC1 · PDBe 3OC1 · UniProt Q16539

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