3ASW | pdb_00003asw

Structural and biochemical characterization of ClfB:ligand interactions

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 
    0.219 (Depositor), 0.220 (DCC) 
  • R-Value Work: 
    0.182 (Depositor), 0.180 (DCC) 
  • R-Value Observed: 
    0.184 (Depositor) 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Structural and biochemical characterization of ClfB:ligand interactions

Ganesh, V.K., Barbu, E.M., Deivanayagam, C.C.S., Le, B., Anderson, A., Matsuka, Y., Lin, S.L., Foster, T.J., Narayana, SV.L., Hook, M.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Clumping factor B328Staphylococcus aureus subsp. aureus N315Mutation(s): 1 
Gene Names: clfB, SA2423
UniProt
Find proteins for Q7A382 (Staphylococcus aureus (strain N315))
Explore Q7A382 
Go to UniProtKB:  Q7A382
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ7A382
Sequence Annotations
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  • Reference Sequence

Find similar proteins by:  Sequence   |   3D Structure  

Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Tail region derived peptide15Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P13645 (Homo sapiens)
Explore P13645 
Go to UniProtKB:  P13645
PHAROS:  P13645
GTEx:  ENSG00000186395 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP13645
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free:  0.219 (Depositor), 0.220 (DCC) 
  • R-Value Work:  0.182 (Depositor), 0.180 (DCC) 
  • R-Value Observed: 0.184 (Depositor) 
Space Group: P 43
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 85.598α = 90
b = 85.598β = 90
c = 84.795γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

  • Released Date: 2011-05-04 
    • Deposition Author(s): Ganesh, V.K.

Revision History  (Full details and data files)

  • Version 1.0: 2011-05-04
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references