1czy

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING PEPTIDE

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only pentamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
TNF receptor-associated factor 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 168 amino acids
Theoretical weight: 19.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12933 (Residues: 334-501; Coverage: 34%)
Gene names: TRAF2, TRAP3
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A
Latent membrane protein 1 Chains: D, E
Molecule details ›
Chains: D, E
Length: 8 amino acids
Theoretical weight: 800 Da
Source organism: Human herpesvirus 4 strain B95-8
Expression system: Not provided
UniProt:
  • Canonical: P03230 (Residues: 204-210; Coverage: 2%)
Gene names: BNLF1, LMP1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 56.2Å b: 76.8Å c: 66.9Å
α: 90° β: 93.2° γ: 90°
R-values:
R R work R free
0.206 0.206 0.245
Expression systems:
  • Escherichia coli
  • Not provided