› 5n1u

X-ray diffraction
2.98Å resolution

Structure of xEco2 acetyltransferase domain

Released:
DOI: 10.2210/pdb5n1u/pdb
PDB 5n1u coloured by chain and viewed from the front.
PDB 5n1u coloured by chain and viewed from the side.
PDB 5n1u coloured by chain and viewed from the top.
Source organism: Xenopus laevis
Primary publication:
Structural Basis of Eco1-Mediated Cohesin Acetylation.
Chao WC, Wade BO, Bouchoux C, Jones AW, Purkiss AG, Federico S, O'Reilly N, Snijders AP, Uhlmann F, Singleton MR
Sci Rep 7 44313 (2017)
PMID: 28290497

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase ESCO2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.86 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: A8QZK6 (Residues: 523-702; Coverage: 26%)
Gene name: xeco2
Sequence domains: ESCO1/2 acetyl-transferase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 58.475Å b: 66.287Å c: 109.763Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.223 0.268
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Towards a Structural Mechanism for Sister Chromatid Cohesion Establishment at the Eukaryotic Replication Fork.
Henrikus et al. (2021)
3 other articles

2 mentions without citation

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