1NUE

X-RAY STRUCTURE OF NM23 HUMAN NUCLEOSIDE DIPHOSPHATE KINASE B COMPLEXED WITH GDP AT 2 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.177 
  • R-Value Observed: 0.177 

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This is version 1.3 of the entry. See complete history. 


Literature

X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution.

Morera, S., Lacombe, M.L., Xu, Y., LeBras, G., Janin, J.

(1995) Structure 3: 1307-1314

  • DOI: https://doi.org/10.1016/s0969-2126(01)00268-4
  • Primary Citation of Related Structures:  
    1NUE

  • PubMed Abstract: 

    Nucleoside diphosphate (NDP) kinases provide precursors for DNA and RNA synthesis. In mammals, these enzymes are also involved in cell regulations. Human NDP kinase B, product of the human nm23-H2 gene, is both an enzyme and a transcription factor. It activates transcription of the c-myc oncogene independently of its catalytic function, by binding to its promoter DNA. How do the two functions coexist?

    • Organizational Affiliation: 

    Laboratoire de Biologie Structurale, UMR 9920 CNRS-Université Paris-Sud, Gif-sur-Yvette, France.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NUCLEOSIDE DIPHOSPHATE KINASE
A, B, C, D, E
A, B, C, D, E, F
151Homo sapiensMutation(s): 0 
EC: 2.7.4.6
UniProt & NIH Common Fund Data Resources
Find proteins for P22392 (Homo sapiens)
Explore P22392 
Go to UniProtKB:  P22392
PHAROS:  P22392
GTEx:  ENSG00000243678 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP22392
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.177 
  • R-Value Observed: 0.177 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 70.03α = 90
b = 87.37β = 90
c = 162.1γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1996-04-03
    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: 2024-02-14
    Changes: Data collection, Database references, Derived calculations, Other