PDBsum entry 1cf2

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
Protein chains
336 a.a. *
SO4 ×4
NAP ×4
Waters ×960
* Residue conservation analysis
PDB id:
Name: Oxidoreductase
Title: Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon methanothermus fervidus
Structure: Protein (glyceraldehyde-3-phosphate dehydrogenase). Chain: p, r, o, q. Engineered: yes
Source: Methanothermus fervidus. Organism_taxid: 2180. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PQS)
2.10Å     R-factor:   0.194     R-free:   0.257
Authors: C.Charron,F.Talfournier,M.N.Isuppov,G.Branlant, J.A.Littlechild,B.Vitoux,A.Aubry
Key ref:
C.Charron et al. (1999). Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus. Acta Crystallogr D Biol Crystallogr, 55, 1353-1355. PubMed id: 10393306 DOI: 10.1107/S0907444999005363
24-Mar-99     Release date:   29-Mar-00    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P10618  (G3P_METFE) -  Glyceraldehyde-3-phosphate dehydrogenase
337 a.a.
336 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glyceraldehyde-3-phosphate dehydrogenase (NAD(P)(+)) (phosphorylating).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D- glyceroyl phosphate + NAD(P)H
D-glyceraldehyde 3-phosphate
+ phosphate
Bound ligand (Het Group name = NAP)
corresponds exactly
= 3-phospho-D- glyceroyl phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     oxidoreductase activity     7 terms  


DOI no: 10.1107/S0907444999005363 Acta Crystallogr D Biol Crystallogr 55:1353-1355 (1999)
PubMed id: 10393306  
Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus.
C.Charron, F.Talfournier, M.N.Isupov, G.Branlant, J.A.Littlechild, B.Vitoux, A.Aubry.
The homotetrameric holo-D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus has been crystallized in the presence of NADP+ using the hanging-drop vapour-diffusion method. Crystals grew from a solution containing 2-methyl-2,4-pentanediol and magnesium acetate. A native data set has been collected to 2.1 A using synchrotron radiation and cryocooling. Diffraction data have been processed in the orthorhombic system (space group P21212) with unit-cell dimensions a = 136.7, b = 153.3, c = 74.9 A and one tetramer per asymmetric unit.
  Selected figure(s)  
Figure 1.
Figure 1 Crystals of recombinant M. fervidus GAPDH grown in 2-methyl-2,4-pentanediol, magnesium acetate and cacodylate buffer as described in the text (ten graduations = 0.25 mm).
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1353-1355) copyright 1999.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
16963457 F.Ferreira-da-Silva, P.J.Pereira, L.Gales, M.Roessle, D.I.Svergun, P.Moradas-Ferreira, and A.M.Damas (2006).
The crystal and solution structures of glyceraldehyde-3-phosphate dehydrogenase reveal different quaternary structures.
  J Biol Chem, 281, 33433-33440.
PDB code: 2i5p
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