1KR4

Structure Genomics, Protein TM1056, cutA


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.218 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

X-ray crystal structure of CutA from Thermotoga maritima at 1.4 A resolution.

Savchenko, A.Skarina, T.Evdokimova, E.Watson, J.D.Laskowski, R.Arrowsmith, C.H.Edwards, A.M.Joachimiak, A.Zhang, R.G.

(2004) Proteins 54: 162-165


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Protein TM1056, cutA125Thermotoga maritimaMutation(s): 2 
UniProt
Find proteins for Q9X0E6 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8))
Explore Q9X0E6 
Go to UniProtKB:  Q9X0E6
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9X0E6
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.40 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.218 
  • R-Value Observed: 0.218 
  • Space Group: P 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.237α = 90
b = 52.237β = 90
c = 33.846γ = 120
Software Package:
Software NamePurpose
d*TREKdata scaling
HKL-2000data reduction
CNSrefinement
d*TREKdata reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2002-08-14
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2017-10-11
    Changes: Refinement description