5cq2

X-ray diffraction
1.4Å resolution

Crystal Structure of tandem WW domains of ITCH in complex with TXNIP peptide

Released:

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 analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-188559 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase Itchy homolog Chain: A
Molecule details ›
Chain: A
Length: 90 amino acids
Theoretical weight: 10.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96J02 (Residues: 433-521; Coverage: 10%)
Gene name: ITCH
Sequence domains: WW domain
Structure domains: Ubiquitin Ligase Nedd4; Chain: W;
Thioredoxin-interacting protein Chains: B, C
Molecule details ›
Chains: B, C
Length: 14 amino acids
Theoretical weight: 1.36 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9H3M7 (Residues: 327-338; Coverage: 3%)
Gene names: TXNIP, VDUP1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 57.277Å b: 62.26Å c: 67.815Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.184
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided