2G9Z

Thiamin pyrophosphokinase from Candida albicans

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 

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Ligand Structure Quality Assessment 


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


Literature

Structural characterization of CA1462, the Candida albicans thiamine pyrophosphokinase.

Santini, S., Monchois, V., Mouz, N., Sigoillot, C., Rousselle, T., Claverie, J.M., Abergel, C.

(2008) BMC Struct Biol 8: 33-33

  • DOI: https://doi.org/10.1186/1472-6807-8-33
  • Primary Citation of Related Structures:  
    2G9Z, 2HH9

  • PubMed Abstract: 

    In search of new antifungal targets of potential interest for pharmaceutical companies, we initiated a comparative genomics study to identify the most promising protein-coding genes in fungal genomes. One criterion was the protein sequence conservation between reference pathogenic genomes. A second criterion was that the corresponding gene in Saccharomyces cerevisiae should be essential. Since thiamine pyrophosphate is an essential product involved in a variety of metabolic pathways, proteins responsible for its production satisfied these two criteria.

    • Organizational Affiliation: 

    Information Genomique et Structurale, UPR2589, Parc Scientifique de Luminy, 13288, Marseille cedex 09, France. santini.s@fsagx.ac.be


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
thiamine pyrophosphokinase
A, B
348Candida albicansMutation(s): 0 
Gene Names: CA1462
EC: 2.7.6.2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
VNP
Query on VNP
Download Ideal Coordinates CCD File 
H [auth A],
N [auth B]		3-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-(2-{[HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]OXY}ETHYL)-4-METHYL-1,3-THIAZOL-3-I UM
C12 H20 N5 O6 P2 S
LWNISHVQCROCTL-UHFFFAOYSA-O
PO4
Query on PO4
Download Ideal Coordinates CCD File 
G [auth A],
M [auth B]		PHOSPHATE ION
O4 P
NBIIXXVUZAFLBC-UHFFFAOYSA-K
CL
Query on CL
Download Ideal Coordinates CCD File 
F [auth A],
L [auth B]		CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
MG
Query on MG
Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
I [auth B]
J [auth B]
C [auth A],
D [auth A],
E [auth A],
I [auth B],
J [auth B],
K [auth B]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.236 
  • R-Value Work: 0.187 
  • R-Value Observed: 0.187 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.825α = 66.14
b = 60.331β = 89.94
c = 63.722γ = 65.07
Software Package:
Software NamePurpose
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing
REFMACrefinement
CCP4data scaling

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-04-04
    Type: Initial release
  • Version 1.1: 2008-02-19
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2023-10-25
    Changes: Data collection, Database references, Derived calculations, Refinement description, Structure summary