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PDBsum entry 1szj

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protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1szj
Jmol
Contents
Protein chains
333 a.a. *
Ligands
SO4 ×4
NAD ×2
Waters ×366
* Residue conservation analysis
PDB id:
1szj
Name: Oxidoreductase
Title: Structure of holo-glyceraldehyde-3-phosphate-dehydrogenase f palinurus versicolor refined 2.0 angstrom resolution
Structure: D-glyceraldehyde-3-phosphate-dehydrogenase. Chain: g, r. Fragment: NAD+ binding domain and catalytic domain. Other_details: complex with NAD+
Source: Palinurus versicolor. South china sea lobster. Organism_taxid: 82835. Organ: tail. Tissue: tail muscle
Biol. unit: Tetramer (from PQS)
Resolution:
2.00Å     R-factor:   0.168     R-free:   0.223
Authors: S.Song,J.Li,Z.Lin
Key ref:
S.Y.Song et al. (1983). Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative. J Mol Biol, 171, 225-228. PubMed id: 6655693 DOI: 10.1016/S0022-2836(83)80355-6
Date:
04-Feb-97     Release date:   16-Sep-98    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P56649  (G3P_PANVR) -  Glyceraldehyde-3-phosphate dehydrogenase
Seq:
Struc:
333 a.a.
333 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.2.1.12  - Glyceraldehyde-3-phosphate dehydrogenase (phosphorylating).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Glyceraldehyde-3-phosphate Dehydrogenase (phosphorylating)
      Reaction: D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH
D-glyceraldehyde 3-phosphate
+ phosphate
+
NAD(+)
Bound ligand (Het Group name = NAD)
corresponds exactly
= 3-phospho-D-glyceroyl phosphate
+ NADH
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   3 terms 
  Biochemical function     oxidoreductase activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1016/S0022-2836(83)80355-6 J Mol Biol 171:225-228 (1983)
PubMed id: 6655693  
 
 
Preliminary crystallographic studies of lobster D-glyceraldehyde-3-phosphate dehydrogenase and the modified enzyme carrying the fluorescent derivative.
S.Y.Song, Y.G.Gao, J.M.Zhou, C.L.Tsou.
 
  ABSTRACT  
 
When the active-site carboxymethylated D-glyceraldehyde-3-phosphate dehydrogenase is irradiated with ultraviolet light in the presence of NAD+, a fluorescent NAD derivative that is covalently linked to the enzyme is obtained. A preliminary crystallographic study of this fluorescent derivative, as well as of the native and the carboxymethylated enzymes from Palinurus versicolor, showed that they are isomorphous and belong to space group C2 as reported for the native enzyme from Palinurus vulgaris. The three forms of the enzyme, although they have identical unit cell parameters, differ considerably in their diffraction patterns, indicating marked differences in conformation in spite of the fact that they differ chemically only in a restricted region around the active site.
 
  Selected figure(s)  
 
Figure 1.
FIo. 1. A comparison of the precession photographs of native, carboxymethylated and fluorescent derivative of v-glyceraldehyde-3-phosphate dehydrogenase. (a)Native enzyme, hO1; (b)native enzyme, hk0; (c) carboxymethylated enzyme, hk0; (d) enzyme carrying the fluorescent derivative, hk0.
 
  The above figure is reprinted by permission from Elsevier: J Mol Biol (1983, 171, 225-228) copyright 1983.