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P38ALPHA MAP kinase bound to cmpd 2

Analyse P38ALPHA MAP kinase bound to cmpd 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AA0
Type: protein
Length: 328 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, 2.7.1.37
UniProt: Q16539
Ligands: AA0
Pockets: 5 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24, 2.7.1.37)	protein	328	39% helix, 16% strand	Q16539

Ligands and binding sites

AA0 · N-[4-methyl-3-[6-(4-methylpiperazin-1-yl)-4-oxidanylidene-quinazolin-3-yl]phenyl]-2-morpholin-4-yl-pyridine-4-carboxamide · 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	436	0.71	0.81	41	AA0
2	74	0.34	0.76	18	empty
3	83	0.33	0.74	16	empty
4	68	0.30	0.73	16	empty
5	50	0.25	0.73	13	empty

Compared structures

4AA0 · P38ALPHA MAP kinase bound to cmpd 2 · 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 4AA0 · PDBe 4AA0 · UniProt Q16539

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