3KDF

X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.98 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.192 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

X-ray Crystal Structure of the Human Replication Protein A Complex from Wheat Germ Cell Free Expression

Makino, S.-I.Burgie, E.S.Bingman, C.A.Fox, B.G.Phillips Jr., G.N.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Replication protein A 14 kDa subunit
A, C
121Homo sapiensMutation(s): 1 
Gene Names: REPA3RPA14RPA3
UniProt & NIH Common Fund Data Resources
Find proteins for P35244 (Homo sapiens)
Explore P35244 
Go to UniProtKB:  P35244
PHAROS:  P35244
GTEx:  ENSG00000106399 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP35244
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Replication protein A 32 kDa subunitB [auth D],
D [auth B]
132Homo sapiensMutation(s): 1 
Gene Names: REPA2RPA2RPA32RPA34
UniProt & NIH Common Fund Data Resources
Find proteins for P15927 (Homo sapiens)
Explore P15927 
Go to UniProtKB:  P15927
PHAROS:  P15927
GTEx:  ENSG00000117748 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15927
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.98 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.192 
  • R-Value Observed: 0.192 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 66.68α = 90
b = 77.7β = 90
c = 121.3γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
DMphasing
PHENIXrefinement
PDB_EXTRACTdata extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-12-01
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2017-11-01
    Changes: Refinement description
  • Version 1.3: 2021-10-13
    Changes: Database references, Derived calculations