3U6U

Crystal structure of the putative acetylglutamate kinase from thermus thermophilus


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.92 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.225 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The structure of first dimeric archaeal N-acetyl glutamate kinase reveals an intermediate conformation of the enzyme in the catalytic cycle

Ramya, S.Preethi, R.Kuramitsu, S.Yokoyama, S.Kumarevel, T.S.Karthe, P.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative acetylglutamate kinaseA,
B [auth C]
269Thermus thermophilus HB8Mutation(s): 0 
Gene Names: TTHA1903
UniProt
Find proteins for Q5SH27 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q5SH27 
Go to UniProtKB:  Q5SH27
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ5SH27
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.92 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.222 
  • R-Value Observed: 0.225 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 155.601α = 90
b = 155.601β = 90
c = 79.535γ = 120
Software Package:
Software NamePurpose
BSSdata collection
SOLVEphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2011-11-16
    Type: Initial release
  • Version 1.1: 2024-03-20
    Changes: Data collection, Database references, Derived calculations