1WKG

Acetylornithine aminotransferase from thermus thermophilus HB8


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.226 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Acetylornithine aminotransferase from thermus thermophilus HB8

Matsumura, M.Goto, M.Omi, R.Miyahara, I.Hirotsu, K.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Acetylornithine/acetyl-lysine aminotransferase
A, B
395Thermus thermophilusMutation(s): 0 
EC: 2.6.1.11
UniProt
Find proteins for Q5SHH5 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SHH5 
Go to UniProtKB:  Q5SHH5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SHH5
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
POI
Query on POI

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
N~2~-ACETYL-N~5~-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-ORNITHINE
C15 H24 N3 O8 P
QIZZUQLTAZUUFQ-ZDUSSCGKSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.226 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 71.27α = 90
b = 69.79β = 90
c = 140.5γ = 90
Software Package:
Software NamePurpose
AMoREphasing
CNSrefinement

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-09-27
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description
  • Version 1.4: 2024-03-13
    Changes: Data collection, Database references, Derived calculations