MolNFT v1 · #129049 · protein

Covalent inhibitor 4B bound to the lipid pocket of P38ALPHA mutant S252C

5O8U · Mitogen-activated protein kinase 14: “Covalent inhibitor 4B bound to the lipid pocket of P38ALPHA mutant S252C”. X-ray diffraction, 1 ligand (9O5), 5 pockets (best druggability 0.70). MolNFT v1 #129049 on GenesisL1: 3D structure…

PDB: 5O8U
Type: protein
Length: 331 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: 9O5
Pockets: 5 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	331	41% helix, 15% strand	Q16539

Ligands and binding sites

9O5 · 4-[3-[7-azanyl-4-(2-phenylethylamino)quinazolin-2-yl]phenyl]butan-2-one · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.70	0.89	24	9O5
2	413	0.65	0.78	39	empty
3	75	0.36	0.76	21	empty
4	60	0.30	0.75	14	empty
5	68	0.29	0.73	14	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5O8U · Covalent Inhibitor 4b bound to the Lipid Pocket of p38alpha Mutant S252C · 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 5O8U · PDBe 5O8U · UniProt Q16539

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