Research workbench

Human P38 MAP kinase in complex with np-F2 and RL87

Analyse Human P38 MAP kinase in complex with np-F2 and RL87 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EH3
Type: protein
Length: 339 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: NAR, IRG
Pockets: 7 · best druggability 0.67

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)	protein	339	40% helix, 16% strand	Q16539

Ligands and binding sites

NAR · Naringenin · ligand · chains A
IRG · N~4~-cyclopropyl-2-phenylquinazoline-4,7-diamine · ligand · chains A

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

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	206	0.67	0.85	29	NAR
2	123	0.65	0.88	20	IRG
3	230	0.60	0.80	31	empty
4	156	0.46	0.76	26	empty
5	113	0.40	0.75	20	empty

Compared structures

4EH3 · Human p38 MAP kinase in complex with NP-F2 and RL87 · 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 4EH3 · PDBe 4EH3 · UniProt Q16539

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