3FO5

Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.205 

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Ligand Structure Quality Assessment 


This is version 1.3 of the entry. See complete history. 


Literature

Comparative structural analysis of lipid binding START domains.

Thorsell, A.G., Lee, W.H., Persson, C., Siponen, M.I., Nilsson, M., Busam, R.D., Kotenyova, T., Schuler, H., Lehtio, L.

(2011) PLoS One 6: e19521-e19521

  • DOI: https://doi.org/10.1371/journal.pone.0019521
  • Primary Citation of Related Structures:  
    2PSO, 2R55, 3FO5, 3P0L

  • PubMed Abstract: 

    Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease.

    • Organizational Affiliation: 

    Department of Medical Biochemistry and Biophysics, Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Thioesterase, adipose associated, isoform BFIT2
A, B
258Homo sapiensMutation(s): 0 
Gene Names: ACOT11, hCG_33028, RP11-240D10.1-002
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for Q8WXI4 (Homo sapiens)
Explore Q8WXI4 
Go to UniProtKB:  Q8WXI4
PHAROS:  Q8WXI4
GTEx:  ENSG00000162390 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8WXI4
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.251 
  • R-Value Work: 0.202 
  • R-Value Observed: 0.205 
  • Space Group: C 2 2 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 52.44α = 90
b = 130.08β = 90
c = 165.23γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
PHASERphasing
REFMACrefinement
XDSdata reduction
XSCALEdata scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-02-24
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2011-09-21
    Changes: Database references
  • Version 1.3: 2024-03-20
    Changes: Data collection, Database references, Derived calculations