3m1d

X-ray diffraction
2Å resolution

Structure of BIR1 from cIAP1

Released:
Source organism: Homo sapiens
Primary publication:
Asymmetric recruitment of cIAPs by TRAF2.
J Mol Biol 400 8-15 (2010)
PMID: 20447407

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Baculoviral IAP repeat-containing protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 85 amino acids
Theoretical weight: 9.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13490 (Residues: 40-119; Coverage: 13%)
Gene names: API1, BIRC2, MIHB, RNF48
Sequence domains: Inhibitor of Apoptosis domain
Structure domains: Inhibitor Of Apoptosis Protein (2mihbC-IAP-1); Chain A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: I4122
Unit cell:
a: 59.18Å b: 59.18Å c: 199.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.232
Expression system: Escherichia coli