› 5t53

X-ray diffraction
2.7Å resolution

MOLECULAR BASIS FOR COHESIN ACETYLATION BY ESTABLISHMENT OF SISTER CHROMATID COHESION N-ACETYLTRANSFERASE ESCO1

Released:
DOI: 10.2210/pdb5t53/pdb
PDB entry 5t53 coloured by chain, front view.
PDB entry 5t53 coloured by chain, side view.
PDB entry 5t53 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular Basis for Cohesin Acetylation by Establishment of Sister Chromatid Cohesion N-Acetyltransferase ESCO1.
Rivera-Colón Y, Maguire A, Liszczak GP, Olia AS, Marmorstein R
J Biol Chem 291 26468-26477 (2016)
PMID: 27803161

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-177127 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase ESCO1 Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 26.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5FWF5 (Residues: 599-825; Coverage: 27%)
Gene names: EFO1, ESCO1, KIAA1911
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand ACO 1 x ACO
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I41
Unit cell:
a: 115.556Å b: 115.556Å c: 61.152Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.25 0.285
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases.
He et al. (2018)
6 other articles

1 mention without citation

Molecular Basis for Cohesin Acetylation by Establishment of Sister Chromatid Cohesion N-Acetyltransferase ESCO1.
Rivera-Colón et al. (2016)