4U9Y

Structure of the alpha-tubulin acetyltransferase alpha-TAT1/Mec-17 in complex with CoA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 

Starting Model: experimental
View more details

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

Structure of the alpha-tubulin acetyltransferase alpha-TAT1/Mec-17 in complex with CoA

Yuzawa, S.Kamakura, S.Sumimoto, H.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-tubulin N-acetyltransferase 1201Homo sapiensMutation(s): 0 
Gene Names: ATAT1C6orf134MEC17Nbla00487
EC: 2.3.1.108
UniProt & NIH Common Fund Data Resources
Find proteins for Q5SQI0 (Homo sapiens)
Explore Q5SQI0 
Go to UniProtKB:  Q5SQI0
PHAROS:  Q5SQI0
GTEx:  ENSG00000137343 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SQI0
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 42.849α = 90
b = 121.938β = 90
c = 37.397γ = 90
Software Package:
Software NamePurpose
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
Cootdata extraction
PHENIXrefinement
HKLdata reduction
HKLdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-08-12
    Type: Initial release
  • Version 1.1: 2020-01-29
    Changes: Data collection, Derived calculations
  • Version 1.2: 2023-11-08
    Changes: Data collection, Database references, Refinement description