3O47 | pdb_00003o47

Crystal structure of ARFGAP1-ARF1 fusion protein


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 
    0.243 (Depositor), 0.250 (DCC) 
  • R-Value Work: 
    0.206 (Depositor), 0.220 (DCC) 
  • R-Value Observed: 
    0.207 (Depositor) 

Starting Models: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted GDPClick on this verticalbar to view details

This is version 1.4 of the entry. See complete history


Literature

Crystal structure of ARFGAP1-ARF1 fusion protein

Wang, H.Tong, Y.Nedyalkova, L.Tempel, W.Guan, X.Crombet, L.Arrowsmith, C.H.Edwards, A.M.Bountra, C.Weigelt, J.Bochkarev, A.Park, H.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ADP-ribosylation factor GTPase-activating protein 1, ADP-ribosylation factor 1
A, B
329Homo sapiensMutation(s): 0 
Gene Names: ARFGAP1ARF1GAPARF1
EC: 3.6.5.2
UniProt & NIH Common Fund Data Resources
Find proteins for P84077 (Homo sapiens)
Explore P84077 
Go to UniProtKB:  P84077
PHAROS:  P84077
GTEx:  ENSG00000143761 
Find proteins for Q8N6T3 (Homo sapiens)
Explore Q8N6T3 
Go to UniProtKB:  Q8N6T3
PHAROS:  Q8N6T3
GTEx:  ENSG00000101199 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP84077Q8N6T3
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free:  0.243 (Depositor), 0.250 (DCC) 
  • R-Value Work:  0.206 (Depositor), 0.220 (DCC) 
  • R-Value Observed: 0.207 (Depositor) 
Space Group: I 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.298α = 90
b = 129.161β = 90
c = 157.685γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
PHASERphasing
BUSTER-TNTrefinement
PDB_EXTRACTdata extraction
BUSTERrefinement

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted GDPClick on this verticalbar to view details

Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2010-08-11
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-08-09
    Changes: Refinement description, Source and taxonomy
  • Version 1.3: 2017-11-08
    Changes: Refinement description
  • Version 1.4: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description