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The crystal structure of JNK3 in complex with a phenantroline inhibitor

Analyse The crystal structure of JNK3 in complex with a phenantroline inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1PMU
Type: protein
Length: 342 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 10
EC: 2.7.1.-
UniProt: P53779
Ligands: 9HP, CL
Pockets: 1 · best druggability 0.62

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 10 (EC 2.7.1.-)	protein	342	41% helix, 15% strand	P53779

Ligands and binding sites

9HP · 9-(4-hydroxyphenyl)-2,7-phenanthroline · 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

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	288	0.62	0.80	45	9HP

Compared structures

1PMU · The crystal structure of JNK3 in complex with a phenantroline inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
P53779 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 10 (P53779) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P53779
Elsewhere: RCSB PDB 1PMU · PDBe 1PMU · UniProt P53779

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