› 4mxe

X-ray diffraction
2.6Å resolution

Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA

Released:
DOI: 10.2210/pdb4mxe/pdb
PDB entry 4mxe coloured by chain, front view.
PDB entry 4mxe coloured by chain, side view.
PDB entry 4mxe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Sister Chromatid Cohesion Establishment Factor ESCO1 Operates by Substrate-Assisted Catalysis.
Kouznetsova E, Kanno T, Karlberg T, Thorsell AG, Wisniewska M, Kursula P, Sjögren C, Schüler H
Structure 24 789-796 (2016)
PMID: 27112597

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-177128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase ESCO1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5FWF5 (Residues: 654-836; Coverage: 22%)
Gene names: EFO1, ESCO1, KIAA1911
Sequence domains: ESCO1/2 acetyl-transferase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P41212
Unit cell:
a: 66.333Å b: 66.333Å c: 211.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.221 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Esco1 and Esco2 regulate distinct cohesin functions during cell cycle progression.
Alomer et al. (2017)
4 more

1 mention without citation

Structural Basis of Eco1-Mediated Cohesin Acetylation.
Chao et al. (2017)