MolNFT v1 · #73764 · protein

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

3OC1 · Mitogen-activated protein kinase 14: “Conformational plasticity of P38 MAP kinase dfg motif mutants in response to inhibitor binding”. X-ray diffraction, 1 ligand (BMU), 6 pockets (best druggability 0.69). MolNFT v1 #73764 on…

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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