› 5an4

X-ray diffraction
1.6Å resolution

Crystal structure of the human 8-oxoguanine glycosylase (OGG1) processed with the CrystalDirect automated mounting and cryo-cooling technology

Released:
DOI: 10.2210/pdb5an4/pdb
PDB entry 5an4 coloured by chain, front view.
PDB entry 5an4 coloured by chain, side view.
PDB entry 5an4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Automated harvesting and processing of protein crystals through laser photoablation.
Zander U, Hoffmann G, Cornaciu I, Marquette JP, Papp G, Landret C, Seroul G, Sinoir J, Röwer M, Felisaz F, Rodriguez-Puente S, Mariaule V, Murphy P, Mathieu M, Cipriani F, Márquez JA
Acta Crystallogr D Struct Biol 72 454-66 (2016)
PMID: 27050125

Function and Biology Details

Reaction catalysed: 
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-glycosylase/DNA lyase Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 35.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15527 (Residues: 12-323; Coverage: 90%)
Gene names: MMH, MUTM, OGG1, OGH1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P65
Unit cell:
a: 106.071Å b: 106.071Å c: 47.287Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.184 0.214
Expression system: Escherichia coli

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Citations

2 review citations

Protein X-ray Crystallography and Drug Discovery.
Maveyraud et al. (2020)
1 more

2 mentions without citation

Automated harvesting and processing of protein crystals through laser photoablation.
Zander et al. (2016)
1 more