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

Analyse Conformational plasticity of P38 MAP kinase dfg 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: 3OBJ
Type: protein
Length: 332 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 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	332	38% helix, 15% 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
BOG · octyl beta-D-glucopyranoside · 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	536	0.73	0.81	57	BMU
2	221	0.68	0.85	31	BOG
3	114	0.41	0.76	16	empty
4	71	0.34	0.75	12	empty
5	61	0.31	0.75	19	empty

Compared structures

3OBJ · Conformational plasticity of p38 MAP kinase DFG mutants in response to inhibitor binding · 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 3OBJ · PDBe 3OBJ · UniProt Q16539

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