7tmx

X-ray diffraction
2.3Å resolution

Structure of Mouse Importin alpha NEIL1 NLS Peptide Complex

Released:
Model geometry
Fit model/data
Source organisms:
Primary publication:
Structural basis of nuclear transport for NEIL DNA glycosylases mediated by importin-alpha.
Biochim Biophys Acta Proteins Proteom 1872 140974 (2023)
PMID: 38065227

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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-223813 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Importin subunit alpha-1 Chain: I
Molecule details ›
Chain: I
Length: 460 amino acids
Theoretical weight: 49.89 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P52293 (Residues: 70-529; Coverage: 87%)
Gene names: Kpna2, Rch1
Sequence domains:
Endonuclease 8-like 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 20 amino acids
Theoretical weight: 2.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96FI4 (Residues: 359-378; Coverage: 5%)
Gene name: NEIL1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 78.541Å b: 90.378Å c: 99.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.22 0.254
Expression systems:
  • Escherichia coli
  • Not provided