› 1ify

Solution NMR

Solution Structure of the Internal UBA Domain of HHR23A

Released:
DOI: 10.2210/pdb1ify/pdb
PDB entry 1ify coloured by chain, ensemble of 10 models, front view.
PDB entry 1ify coloured by chain, ensemble of 10 models, side view.
PDB entry 1ify coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structures of UBA domains reveal a conserved hydrophobic surface for protein-protein interactions.
Mueller TD, Feigon J
J Mol Biol 319 1243-55 (2002)
PMID: 12079361

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
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: 49 amino acids
Theoretical weight: 5.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54725 (Residues: 156-204; Coverage: 14%)
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
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins.
Hicke et al. (2003)
18 more

11 mentions without citation

Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein.
Timm et al. (2008)
10 more