6SP0

Structure of Esco2 acetyltransferase in complex with CoA

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.198 
  • R-Value Work: 0.169 

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This is version 1.1 of the entry. See complete history. 


Literature

Alternative catalytic residues in the active site of Esco acetyltransferases

Ajam, T., De, I., Petkau, N., Whelan, G., Pena, V., Eichele, G.

(2020) Sci Rep 


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-acetyltransferase ESCO2226Mus musculusMutation(s): 0 
Gene Names: Esco2
EC: 2.3.1
UniProt
Find proteins for Q8CIB9 (Mus musculus)
Explore Q8CIB9 
Go to UniProtKB:  Q8CIB9
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8CIB9
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.77 Å
  • R-Value Free: 0.198 
  • R-Value Work: 0.169 
  • Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.68α = 90
b = 52.68β = 90
c = 107.47γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PHENIXrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
XDSdata scaling
PHENIXphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2020-07-01
    Type: Initial release
  • Version 1.1: 2024-05-15
    Changes: Advisory, Data collection, Database references