6CVZ

Crystal structure of the WD40-repeat of RFWD3


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.215 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Target highlights in CASP13: Experimental target structures through the eyes of their authors.

Lepore, R.Kryshtafovych, A.Alahuhta, M.Veraszto, H.A.Bomble, Y.J.Bufton, J.C.Bullock, A.N.Caba, C.Cao, H.Davies, O.R.Desfosses, A.Dunne, M.Fidelis, K.Goulding, C.W.Gurusaran, M.Gutsche, I.Harding, C.J.Hartmann, M.D.Hayes, C.S.Joachimiak, A.Leiman, P.G.Loppnau, P.Lovering, A.L.Lunin, V.V.Michalska, K.Mir-Sanchis, I.Mitra, A.K.Moult, J.Phillips Jr., G.N.Pinkas, D.M.Rice, P.A.Tong, Y.Topf, M.Walton, J.D.Schwede, T.

(2019) Proteins 87: 1037-1057

  • DOI: https://doi.org/10.1002/prot.25805
  • Primary Citation of Related Structures:  
    6CVZ, 6SD8, 6SDA

  • PubMed Abstract: 

    The functional and biological significance of selected CASP13 targets are described by the authors of the structures. The structural biologists discuss the most interesting structural features of the target proteins and assess whether these features were correctly reproduced in the predictions submitted to the CASP13 experiment.


  • Organizational Affiliation

    BSC-CNS Barcelona Supercomputing Center, Barcelona, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
E3 ubiquitin-protein ligase RFWD3
A, B, C
351Homo sapiensMutation(s): 0 
Gene Names: RFWD3RNF201
EC: 2.3.2.27
UniProt & NIH Common Fund Data Resources
Find proteins for Q6PCD5 (Homo sapiens)
Explore Q6PCD5 
Go to UniProtKB:  Q6PCD5
PHAROS:  Q6PCD5
GTEx:  ENSG00000168411 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ6PCD5
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.239 
  • R-Value Work: 0.214 
  • R-Value Observed: 0.215 
  • Space Group: P 32
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 91.991α = 90
b = 91.991β = 90
c = 110.738γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
SCALEPACKdata scaling
PHASERphasing
PDB_EXTRACTdata extraction

Structure Validation

View Full Validation Report



Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2018-06-27
    Type: Initial release
  • Version 1.1: 2021-09-22
    Changes: Database references, Derived calculations