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P38ALPHA MAP kinase bound to cmpd 29

Analyse P38ALPHA MAP kinase bound to cmpd 29 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AAC
Type: protein
Length: 350 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: AAV, CL
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	350	38% helix, 15% strand	Q16539

Ligands and binding sites

AAV · N-isoxazol-3-yl-4-methyl-3-[6-(4-methylpiperazin-1-yl)-4-oxo-quinazolin-3-yl]benzamide · ligand · chains A
CL · Chloride ion · ion · 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	299	0.67	0.82	34	AAV
2	241	0.53	0.76	39	empty
3	109	0.38	0.74	17	empty
4	58	0.34	0.78	15	empty
5	50	0.33	0.78	16	empty

Compared structures

4AAC · P38ALPHA MAP kinase bound to cmpd 29 · 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 4AAC · PDBe 4AAC · UniProt Q16539

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