› 2m65

Solution NMR

NMR structure of human restriction factor APOBEC3A

Released:
DOI: 10.2210/pdb2m65/pdb
PDB entry 2m65 coloured by chain, ensemble of 30 models, front view.
PDB entry 2m65 coloured by chain, ensemble of 30 models, side view.
PDB entry 2m65 coloured by chain, ensemble of 30 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.
Byeon IJ, Ahn J, Mitra M, Byeon CH, Hercík K, Hritz J, Charlton LM, Levin JG, Gronenborn AM
Nat Commun 4 1890 (2013)
PMID: 23695684

Function and Biology Details

Reaction catalysed: 
Cytosine in single-stranded DNA + H(2)O = uracil in single-stranded DNA + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152109 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA dC->dU-editing enzyme APOBEC-3A Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 24.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31941 (Residues: 1-199; Coverage: 100%)
Gene name: APOBEC3A
Sequence domains: APOBEC-like C-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 67%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Mechanisms underlying mutational signatures in human cancers.
Helleday et al. (2014)
15 more

21 mentions without citation

The APOBEC Protein Family: United by Structure, Divergent in Function.
Salter et al. (2016)
20 more