MolNFT v1 · #126071 · protein

Structure of A20 otu domain bound to ubiquitin

5LRX: “Structure of A20 otu domain bound to ubiquitin”. X-ray diffraction, 1 ligand (AYE). MolNFT v1 #126071 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5LRX
Type: protein
Length: 1,511 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P21580, P0CG47
Ligands: AYE

Structure

x-ray diffraction · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	348	—	P21580
B, D	—	protein	75	—	P0CG47
C	—	protein	346	—	P21580
E	—	protein	338	—	P21580
F	—	protein	329	—	P21580

Ligands and binding sites

AYE · prop-2-en-1-amine · ligand · 2 copies · chains A, B, C, D

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

Compared structures

5LRX · Structure of A20 OTU domain bound to ubiquitin · the same entry in another collection · chain F against F, TM-score 1.00
P21580 · AlphaFold monomer V2.0 prediction for tumor necrosis factor alpha- induced protein 3… · a predicted model of the same protein · chain C 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 P21580
Every structure of UniProt P0CG47
Elsewhere: RCSB PDB 5LRX · PDBe 5LRX · UniProt P21580 · UniProt P0CG47

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