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Crystal structure of the C2 domain of human itchy homolog E3 ubiquitin protein ligase

Analyse Crystal structure of the C2 domain of human itchy homolog E3 ubiquitin protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2NQ3
Type: protein
Length: 131 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Itchy homolog E3 ubiquitin protein ligase
EC: 6.3.2.-
UniProt: Q96J02
Ligands: CL
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Itchy homolog E3 ubiquitin protein ligase (EC 6.3.2.-)	protein	131	5% helix, 56% strand	Q96J02

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.29	0.74	13	empty

Compared structures

2NQ3 · Crystal structure of the C2 Domain of Human Itchy Homolog E3 Ubiquitin Protein 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 0.99

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 Q96J02
Elsewhere: RCSB PDB 2NQ3 · PDBe 2NQ3 · UniProt Q96J02

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