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Crystal structure of FUS3 phosphorylated on TYR182

Analyse Crystal structure of FUS3 phosphorylated on TYR182 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F9G
Type: protein
Length: 332 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	332	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	233	0.63	0.82	31	MG, ADP
2	93	0.41	0.77	21	empty
3	68	0.39	0.79	16	empty

Compared structures

2F9G · Crystal structure of Fus3 phosphorylated on Tyr182 · 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 2F9G · PDBe 2F9G · UniProt P16892

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