Research workbench

Crystal structure of AMP-bound human JNK2

Analyse Crystal structure of AMP-bound human JNK2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7N8T
Type: protein
Length: 355 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase 9
EC: 2.7.11.24
UniProt: P45984
Ligands: AMP
Pockets: 3 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase 9 (EC 2.7.11.24)	protein	355	38% helix, 16% strand	P45984

Ligands and binding sites

AMP · Adenosine monophosphate · ligand · chains A
P6G · Hexaethylene glycol · additive · 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	693	0.76	0.81	65	AMP
2	190	0.50	0.76	19	empty
3	86	0.33	0.74	18	empty

Compared structures

7N8T · Crystal Structure of AMP-bound Human JNK2 · the same entry in another collection · chain A against A, TM-score 1.00
P45984 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 9 (P45984) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P45984
Elsewhere: RCSB PDB 7N8T · PDBe 7N8T · UniProt P45984

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