3BYI

Crystal structure of human Rho GTPase activating protein 15 (ARHGAP15)

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 

wwPDB Validation   3D Report Full Report


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


Literature

Crystal Structure of Human Rho GTPase Activating Protein 15 (ARHGAP15).

Shrestha, L., Tickle, J., Elkins, J., Burgess-Brown, N., Johansson, C., Papagrigoriou, E., Kavanagh, K., Pike, A.C.W., Ugochukwu, E., Uppenberg, J., von Delft, F., Arrowsmith, C.H., Edwards, A.M., Weigelt, J., Doyle, D.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Rho GTPase activating protein 15
A, B, C, D
214Homo sapiensMutation(s): 0 
Gene Names: ARHGAP15
UniProt & NIH Common Fund Data Resources
Find proteins for Q53QZ3 (Homo sapiens)
Explore Q53QZ3 
Go to UniProtKB:  Q53QZ3
PHAROS:  Q53QZ3
GTEx:  ENSG00000075884 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ53QZ3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.25 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.191 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 120.618α = 90
b = 130.142β = 90
c = 62.477γ = 90
Software Package:
Software NamePurpose
SCALAdata scaling
PHASERphasing
REFMACrefinement
PDB_EXTRACTdata extraction
CrystalCleardata collection
MOSFLMdata reduction

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-02-26
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2023-08-30
    Changes: Data collection, Database references, Refinement description