› 6e5x

X-ray diffraction
1.5Å resolution

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:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181206 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcriptional activator VP30 Chain: A
Molecule details ›
Chain: A
Length: 127 amino acids
Theoretical weight: 14.41 KDa
Source organism: Ebola virus - Zaire (1995)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q77DJ5 (Residues: 140-266; Coverage: 44%)
Gene name: VP30
Sequence domains: Ebola virus-specific transcription factor VP30
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)
E3 ubiquitin-protein ligase RBBP6 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q7Z6E9 (Residues: 554-568; Coverage: 1%)
Gene names: My038, P2PR, PACT, RBBP6, RBQ1

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P43212
Unit cell:
a: 45.6Å b: 45.6Å c: 158.71Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.23
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

19 review citations

Deciphering cell-cell interactions and communication from gene expression.
Armingol et al. (2021)
18 more

2 mentions without citation

Protein Interaction Mapping Identifies RBBP6 as a Negative Regulator of Ebola Virus Replication.
Batra et al. (2018)
1 more