1B7G

GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.226 

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This is version 1.4 of the entry. See complete history. 


Literature

Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.

Isupov, M.N., Fleming, T.M., Dalby, A.R., Crowhurst, G.S., Bourne, P.C., Littlechild, J.A.

(1999) J Mol Biol 291: 651-660

  • DOI: https://doi.org/10.1006/jmbi.1999.3003
  • Primary Citation of Related Structures:  
    1B7G

  • PubMed Abstract: 

    The enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from the archaea shows low sequence identity (16-20%) with its eubacterial and eukaryotic counterparts. The crystal structure of the apo GAPDH from Sulfolobus solfataricus has been determined by multiple isomorphous replacement at 2.05 A resolution. The enzyme has several differences in secondary structure when compared with eubacterial GAPDHs, with an overall increase in the number of alpha-helices. There is a relocation of the active-site residues within the catalytic domain of the enzyme. The thermostability of the S. solfataricus enzyme can be attributed to a combination of an ion pair cluster and an intrasubunit disulphide bond.

    • Organizational Affiliation: 

    Schools of Chemistry and Biological Sciences, University of Exeter, Stocker Road, Exeter, EX4 4QD, UK.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE)A [auth O],
B [auth Q]		340Saccharolobus solfataricusMutation(s): 1 
EC: 1.2.1.12
UniProt
Find proteins for P39460 (Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2))
Explore P39460 
Go to UniProtKB:  P39460
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP39460
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4
Download Ideal Coordinates CCD File 
C [auth O]
D [auth O]
E [auth O]
F [auth O]
G [auth O]
C [auth O],
D [auth O],
E [auth O],
F [auth O],
G [auth O],
H [auth O],
I [auth Q],
J [auth Q],
K [auth Q],
L [auth Q],
M [auth Q],
N [auth Q]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.05 Å
  • R-Value Free: 0.293 
  • R-Value Work: 0.226 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 101.55α = 90
b = 101.55β = 90
c = 179.92γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
SHELXmodel building
MLPHAREphasing
REFMACrefinement
SHELXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-10-08
    Type: Initial release
  • Version 1.1: 2007-10-16
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance
  • Version 1.3: 2021-11-03
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-12-27
    Changes: Data collection