MolNFT v1 · #31886 · protein

Crystal structure of non-phosphorylated FUS3

2B9F · Mitogen-activated protein kinase FUS3: “Crystal structure of non-phosphorylated FUS3”. X-ray diffraction, 2 ligands (ADP, MG), 3 pockets (best druggability 0.63). MolNFT v1 #31886 on GenesisL1: 3D structure, binding sites and…

PDB: 2B9F
Type: protein
Length: 337 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Mitogen-activated protein kinase FUS3
EC: 2.7.1.37
UniProt: P16892
Ligands: ADP, MG
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitogen-activated protein kinase FUS3 (EC 2.7.1.37)	protein	337	42% helix, 14% strand	P16892

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 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	296	0.63	0.80	36	MG, ADP
2	97	0.38	0.75	24	empty
3	74	0.36	0.77	21	empty

Compared structures

2B9F · Crystal structure of non-phosphorylated Fus3 · the same entry in another collection · chain A against A, TM-score 1.00
P16892 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase FUS3 (P16892) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P16892
Elsewhere: RCSB PDB 2B9F · PDBe 2B9F · UniProt P16892

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