2CU6

Crystal Structure Of The dTDP-4-keto-L-rhamnose reductase-related Protein From Thermus Thermophilus HB8


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal Structure Of The dTDP-4-keto-L-rhamnose reductase-related Protein From Thermus Thermophilus HB8

Satoh, S.Yokoyama, S.Kuramitsu, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
dTDP-4-keto-L-rhamnose reductase-related Protein
A, B
103Thermus thermophilus HB8Mutation(s): 2 
UniProt
Find proteins for Q53W28 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
Explore Q53W28 
Go to UniProtKB:  Q53W28
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ53W28
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, B
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.215 
  • R-Value Observed: 0.221 
  • Space Group: I 2 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 121.805α = 90
b = 121.805β = 90
c = 121.805γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data reduction
SCALEPACKdata scaling
MOLREPphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-11-25
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Source and taxonomy, Version format compliance