PDBe 4ic3

X-ray diffraction
1.78Å resolution

Crystal structure of the F495L mutant XIAP RING domain

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase XIAP Chains: A, B
Molecule details ›
Chains: A, B
Length: 74 amino acids
Theoretical weight: 8.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 429-497; Coverage: 14%)
Gene names: API3, BIRC4, IAP3, XIAP
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 35.735Å b: 48.471Å c: 39.967Å
α: 90° β: 97.47° γ: 90°
R-values:
R R work R free
0.178 0.176 0.222
Expression system: Escherichia coli