› 2nq3

X-ray diffraction
1.8Å resolution

Crystal structure of the C2 Domain of Human Itchy Homolog E3 Ubiquitin Protein Ligase

Released:
DOI: 10.2210/pdb2nq3/pdb
PDB entry 2nq3 coloured by chain, front view.
PDB entry 2nq3 coloured by chain, side view.
PDB entry 2nq3 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Walker JR, Avvakumov GV, Xue S, Butler-Cole C, Finerty Jr PJ, Weigelt J, Sundstrom M, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, 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
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase Itchy homolog Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 19.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96J02 (Residues: 1-155; Coverage: 17%)
Gene name: ITCH
Sequence domains: C2 domain
Structure domains: C2 domain

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 82.499Å b: 82.499Å c: 65.273Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.164 0.162 0.195
Expression system: Escherichia coli BL21(DE3)

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