› 1dv0

Solution NMR

Refined NMR solution structure of the C-terminal UBA domain of the human homologue of RAD23A (HHR23A)

Released:
DOI: 10.2210/pdb1dv0/pdb
PDB entry 1dv0 coloured by chain, ensemble of 18 models, front view.
PDB entry 1dv0 coloured by chain, ensemble of 18 models, side view.
PDB entry 1dv0 coloured by chain, ensemble of 18 models, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical and structural analysis of the interaction between the UBA(2) domain of the DNA repair protein HHR23A and HIV-1 Vpr.
Withers-Ward ES, Mueller TD, Chen IS, Feigon J
Biochemistry 39 14103-12 (2000)
PMID: 11087358

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157078 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UV excision repair protein RAD23 homolog A Chain: A
Molecule details ›
Chain: A
Length: 47 amino acids
Theoretical weight: 5.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54725 (Residues: 319-363; Coverage: 12%)
Gene name: RAD23A
Sequence domains: UBA/TS-N domain
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
Refinement method: simulated annealing, molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Ubiquitin-binding domains.
Hicke et al. (2005)
7 more

9 mentions without citation

The UBAP1 subunit of ESCRT-I interacts with ubiquitin via a SOUBA domain.
Agromayor et al. (2012)
8 more