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The complex structure of the MAP kinase P38/SB203580

Analyse The complex structure of the MAP kinase P38/SB203580 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1A9U
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: MAP kinase P38
EC: 2.7.1.-
UniProt: Q16539
Ligands: SB2
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	MAP kinase P38 (EC 2.7.1.-)	protein	351	39% helix, 15% strand	Q16539

Ligands and binding sites

SB2 · 4-[5-(4-fluoro-phenyl)-2-(4-methanesulfinyl-phenyl)-3H-imidazol-4-yl]-pyridine · ligand · chains A

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

Pockets

5 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	366	0.65	0.79	39	SB2
2	142	0.49	0.79	20	empty
3	67	0.41	0.80	19	empty
4	113	0.40	0.75	25	empty
5	61	0.29	0.74	16	empty

Compared structures

1A9U · The complex structure of the MAP kinase P38/SB203580 · 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 1A9U · PDBe 1A9U · UniProt Q16539

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