PDBe 2kna

Solution NMR

Solution structure of UBA domain of XIAP

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase XIAP Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P98170 (Residues: 357-449; Coverage: 19%)
Gene names: API3, BIRC4, IAP3, XIAP
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 93%
Refinement method: molecular dynamics
Chemical shifts: BMR16478  
Expression system: Escherichia coli