4j48

X-ray diffraction
2.1Å resolution

Crystal structure of XIAP-BIR2 domain with AMRV bound

Released:

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
Sequence domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase XIAP Chains: A, C
Molecule details ›
Chains: A, C
Length: 86 amino acids
Theoretical weight: 9.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 152-236; Coverage: 17%)
Gene names: API3, BIRC4, IAP3, XIAP
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A
PEPTIDE (ALA-MET-ARG-VAL) Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 477 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I422
Unit cell:
a: 74.805Å b: 74.805Å c: 109.123Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.253
Expression systems:
  • Escherichia coli
  • Not provided