4HNW

The NatA Acetyltransferase Complex Bound To Inositol Hexakisphosphate


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.230 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history


Literature

The Protein Complex NatA Binds Inositol Hexakisphosphate and Exhibits Conformational Flexibility

Neubauer, J.L.Pham, T.Immormino, R.M.Dollins, D.E.Endo-Streeter, S.T.Li, S.Pemble IV, C.W.York, J.D.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
N-terminal acetyltransferase A complex subunit NAT1863Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: NAT1AAA1YDL040CD2720
UniProt
Find proteins for P12945 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P12945 
Go to UniProtKB:  P12945
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP12945
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
N-terminal acetyltransferase A complex catalytic subunit ARD1248Saccharomyces cerevisiae S288CMutation(s): 0 
Gene Names: ARD1YHR013C
EC: 2.3.1.88 (PDB Primary Data), 2.3.1.255 (UniProt)
UniProt
Find proteins for P07347 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P07347 
Go to UniProtKB:  P07347
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07347
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.229 
  • R-Value Observed: 0.230 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 135.662α = 90
b = 135.662β = 90
c = 175.801γ = 120
Software Package:
Software NamePurpose
PHENIXrefinement
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-03-26
    Type: Initial release
  • Version 1.1: 2019-07-17
    Changes: Advisory, Data collection, Refinement description
  • Version 1.2: 2020-10-14
    Changes: Database references, Derived calculations, Structure summary
  • Version 1.3: 2024-02-28
    Changes: Advisory, Data collection, Database references