PDBe 3tug

X-ray diffraction
2.27Å resolution

Crystal structure of the HECT domain of ITCH E3 ubiquitin ligase

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Dobrovetsky E, Xue S, Butler C, Wernimont A, Walker JR, Tempel W, Dhe-Paganon S, Arrowsmith CH, Edwards AM, Bountra C, Tong Y, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
(1a) S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HECT-type E3 ubiquitin transferase]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + S-ubiquitinyl-[HECT-type E3 ubiquitin transferase]-L-cysteine
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Itchy homolog Chain: A
Molecule details ›
Chain: A
Length: 398 amino acids
Theoretical weight: 47.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q96J02 (Residues: 524-903; Coverage: 42%)
Gene name: ITCH
Sequence domains: HECT-domain (ubiquitin-transferase)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3121
Unit cell:
a: 82.779Å b: 82.779Å c: 109.943Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.256
Expression system: Escherichia coli BL21