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Crystal structure of P38ALPHA in complex with SR154

Analyse Crystal structure of P38ALPHA in complex with SR154 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6YJC
Type: protein
Length: 336 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: P47811
Ligands: OSZ
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	336	40% helix, 13% strand	P47811

Ligands and binding sites

OSZ · 5-azanyl-~{N}-[[4-[[(2~{S})-4-cyclohexyl-1-oxidanylidene-1-piperazin-1-yl-butan-2-yl]carbamoyl]phenyl]methyl]-1-phenyl-pyrazole-4-carboxamide · 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	477	0.72	0.82	49	OSZ
2	135	0.42	0.75	20	empty
3	73	0.37	0.77	14	empty
4	80	0.36	0.77	19	EDO
5	63	0.31	0.75	17	empty

Compared structures

6YJC · Crystal structure of p38alpha in complex with SR154 · 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 P47811
Elsewhere: RCSB PDB 6YJC · PDBe 6YJC · UniProt P47811

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