5TTA

A 1.85A X-Ray Structure from Peptoclostridium difficile 630 of a Hypothetical Protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.85 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.182 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

A 1.85A X-Ray Structure from Peptoclostridium difficile 630 of a Hypothetical Protein

Brunzelle, J.S.Minasov, G.Anderson, W.F.Center for Structural Genomics of Infectious Diseases (CSGID)

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Putative exported protein
A, B
248Clostridioides difficile 630Mutation(s): 0 
Gene Names: CD630_21270
UniProt
Find proteins for Q185R5 (Clostridioides difficile (strain 630))
Explore Q185R5 
Go to UniProtKB:  Q185R5
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ185R5
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: 1.85 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.180 
  • R-Value Observed: 0.182 
  • Space Group: P 1
  • Diffraction Data: https://doi.org/10.18430/m35tta
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 30.78α = 73.38
b = 51.04β = 82.06
c = 81.12γ = 86.35
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
PHENIXphasing

Structure Validation

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Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2017-02-01
    Type: Initial release