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P38ALPHA MAP kinase bound to cmpd 33

Analyse P38ALPHA MAP kinase bound to cmpd 33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AA5
Type: protein
Length: 341 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: NQB
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 40% 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	341	40% helix, 16% strand	Q16539

Ligands and binding sites

NQB · N-cyclopropyl-4-methyl-3-[6-(4-methylpiperazin-1-yl)-4-oxidanylidene-quinazolin-3-yl]benzamide · ligand · chains A

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

Pockets

4 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	304	0.68	0.82	37	NQB
2	116	0.38	0.74	16	empty
3	72	0.34	0.76	17	empty
4	56	0.28	0.74	13	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

4AA5 · P38ALPHA MAP kinase bound to cmpd 33 · 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 4AA5 · PDBe 4AA5 · UniProt Q16539

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