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USP14 catalytic domain with IU1

Analyse USP14 catalytic domain with IU1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6IIK
Type: protein
Length: 669 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P54578
Ligands: IU1

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	335	—	P54578
B	—	protein	334	—	P54578

Ligands and binding sites

IU1 · 1-[1-(4-fluorophenyl)-2,5-dimethyl-1H-pyrrol-3-yl]-2-(pyrrolidin-1-yl)ethan-1-one · ligand · 2 copies · chains A, B

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

Compared structures

6IIK · USP14 catalytic domain with IU1 · the same entry in another collection · chain A against A, TM-score 1.00
P54578 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 14 (P54578) · a predicted model of the same protein · chain B 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 P54578
Elsewhere: RCSB PDB 6IIK · PDBe 6IIK · UniProt P54578

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