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Crystal structure of the hect domain of itch E3 ubiquitin ligase

Analyse Crystal structure of the hect domain of itch E3 ubiquitin ligase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TUG
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase itchy homolog
EC: 6.3.2.-
UniProt: Q96J02
Ligands: UNX, CL
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase itchy homolog (EC 6.3.2.-)	protein	334	52% helix, 10% strand	Q96J02

Ligands and binding sites

UNX · Unknown atom or ion · ion · 9 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

2 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	676	0.72	0.79	61	CL, UNX
2	64	0.31	0.75	16	empty

Compared structures

3TUG · Crystal structure of the HECT domain of ITCH E3 ubiquitin ligase · the same entry in another collection · chain A against A, TM-score 1.00
Q96J02 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase itchy homolog (Q96J02) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q96J02
Elsewhere: RCSB PDB 3TUG · PDBe 3TUG · UniProt Q96J02

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