1AD6

DOMAIN A OF HUMAN RETINOBLASTOMA TUMOR SUPPRESSOR


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.201 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box.

Kim, H.Y.Cho, Y.

(1997) Nat Struct Biol 4: 390-395

  • DOI: https://doi.org/10.1038/nsb0597-390
  • Primary Citation of Related Structures:  
    1AD6

  • PubMed Abstract: 

    The pocket region of retinoblastoma tumour suppressor (Rb) is essential for tumour suppressing activity. The Rb pocket is primarily composed of two domains, A and B. We have determined the X-ray crystal structure of domain A (residues 378-562) at 2.3 A resolution. Domain A consists of nine alpha-helices. The overall arrangement of helices in domain A is remarkably similar to the cyclin-box folds found in the crystal structures of cyclin A and TFIIB. This structure, along with domain B which is predicted to be homologous to the cyclin-box, suggests that the Rb pocket is composed of two cyclin-box fold domains. We present the structural/functional features of the Rb pocket, and the potential binding region for cellular or viral proteins within domain A.


  • Organizational Affiliation

    Structural Biology Center, Korea Institute of Science and Technology, Cheongryang, Seoul, South Korea.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
RETINOBLASTOMA TUMOR SUPPRESSOR185Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P06400 (Homo sapiens)
Explore P06400 
Go to UniProtKB:  P06400
PHAROS:  P06400
GTEx:  ENSG00000139687 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06400
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.240 
  • R-Value Work: 0.201 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 38.6α = 90
b = 68.04β = 90
c = 80.83γ = 90
Software Package:
Software NamePurpose
MLPHAREphasing
TNTrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-08-26
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references