Research workbench

Crystal structure of a N-phenyl-N'-naphthylurea analog in complex with P38 MAP kinase

Analyse Crystal structure of a N-phenyl-N'-naphthylurea analog in complex with P38 MAP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GI3
Type: protein
Length: 330 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: B10
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 14 (EC 2.7.11.24)	protein	330	39% helix, 13% strand	Q16539

Ligands and binding sites

B10 · N-{5-tert-butyl-2-methoxy-3-[({4-[6-(morpholin-4-ylmethyl)pyridin-3-yl]naphthalen-1-yl}carbamoyl)amino]phenyl}methanesulfonamide · ligand · chains A

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

Pockets

3 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	566	0.73	0.81	63	B10
2	78	0.40	0.79	16	empty
3	102	0.37	0.75	16	empty

Compared structures

3GI3 · Crystal structure of a N-Phenyl-N'-Naphthylurea analog in complex with p38 MAP kinase · 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 3GI3 · PDBe 3GI3 · UniProt Q16539

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.