6NR1

The X-ray crystal structure of Streptococcus pneumoniae Fatty Acid Kinase (Fak) B2 protein loaded with Vaccenic acid (C18:1 delta11) to 2.1 Angstrom resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.241 
  • R-Value Work: 0.184 
  • R-Value Observed: 0.187 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history


Literature

The X-ray crystal structure of Streptococcus pneumoniae Fatty Acid Kinase (Fak) B2 protein loaded with Vaccenic acid (C18:1 delta11) to 2.1 Angstrom resolution

Cuypers, M.G.Gullett, J.M.Subramanian, C.White, S.W.Rock, C.O.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Fatty Acid Kinase (Fak) B2 protein (SPR1019)
A, B
313Streptococcus pneumoniaeMutation(s): 0 
Gene Names: SPR1019
UniProt
Find proteins for Q8DPT4 (Streptococcus pneumoniae (strain ATCC BAA-255 / R6))
Explore Q8DPT4 
Go to UniProtKB:  Q8DPT4
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8DPT4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.655α = 90
b = 103.409β = 90
c = 107.925γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2019-08-21
    Type: Initial release
  • Version 1.1: 2019-12-18
    Changes: Author supporting evidence
  • Version 1.2: 2023-10-11
    Changes: Data collection, Database references, Refinement description