› 5mea

X-ray diffraction
2.15Å resolution

Crystal structure of yeast Cdt1 (N terminal and middle domain), form 2.

Released:
DOI: 10.2210/pdb5mea/pdb
Model geometry
Fit model/data
PDB entry 5mea coloured by chain, front view.
PDB entry 5mea coloured by chain, side view.
PDB entry 5mea coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Cdt1 stabilizes an open MCM ring for helicase loading.
Frigola J, He J, Kinkelin K, Pye VE, Renault L, Douglas ME, Remus D, Cherepanov P, Costa A, Diffley JFX
OpenAccess logo Nat Commun 8 15720 (2017)
PMID: 28643783

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cell division cycle protein CDT1 Chain: A
Molecule details ›
Chain: A
Length: 439 amino acids
Theoretical weight: 49.48 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P47112 (Residues: 1-438; Coverage: 73%)
Gene names: CDT1, J1641, SID2, TAH11, YJR046W

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 47.51Å b: 89.35Å c: 121.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.249
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The plasticity of DNA replication forks in response to clinically relevant genotoxic stress.
Berti et al. (2020)
9 more

1 mention without citation

Cdt1 stabilizes an open MCM ring for helicase loading.
Frigola et al. (2017)