› 2hlw

Solution NMR

Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a

Released:
DOI: 10.2210/pdb2hlw/pdb
PDB entry 2hlw coloured by chain, ensemble of 15 models, front view.
PDB entry 2hlw coloured by chain, ensemble of 15 models, side view.
PDB entry 2hlw coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains.
Hau DD, Lewis MJ, Saltibus LF, Pastushok L, Xiao W, Spyracopoulos L
Biochemistry 45 9866-77 (2006)
PMID: 16893187

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-conjugating enzyme E2 variant 1 Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 19.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13404 (Residues: 7-147; Coverage: 96%)
Gene names: CROC1, P/OKcl.19, UBE2V, UBE2V1, UEV1
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Anatomy of the E2 ligase fold: implications for enzymology and evolution of ubiquitin/Ub-like protein conjugation.
Burroughs et al. (2008)
6 more

2 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
1 more