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PDBsum entry 1t99

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1t99
Jmol
Contents
Protein chains
256 a.a. *
Ligands
PO4 ×2
Metals
_CD ×2
Waters ×324
* Residue conservation analysis
PDB id:
1t99
Name: Transferase
Title: R106g kdo8ps without substrates
Structure: 2-dehydro-3-deoxyphosphooctonate aldolase. Chain: a, b. Synonym: phospho-2-dehydro-3-deoxyoctonate aldolase, 3-deox octulosonic acid 8-phosphate synthetase, kdo-8-phosphate sy kdo 8-p synthase, kdops. Engineered: yes. Mutation: yes
Source: Aquifex aeolicus. Organism_taxid: 63363. Gene: kdsa, aq_085. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Tetramer (from PDB file)
Resolution:
1.85Å     R-factor:   0.208     R-free:   0.245
Authors: D.L.Gatti
Key ref: X.Xu et al. Effects of the arg106==>gly mutation on the catalytic and conformational cycle of aquifex aeolicus kdo8p synthase.. To be published, .
Date:
16-May-04     Release date:   14-Jun-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O66496  (KDSA_AQUAE) -  2-dehydro-3-deoxyphosphooctonate aldolase
Seq:
Struc:
267 a.a.
256 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.5.1.55  - 3-deoxy-8-phosphooctulonate synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3- deoxy-D-octonate 8-phosphate + phosphate
Phosphoenolpyruvate
+ D-arabinose 5-phosphate
+ H(2)O
= 2-dehydro-3- deoxy-D-octonate 8-phosphate
+
phosphate
Bound ligand (Het Group name = PO4)
corresponds exactly
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     metabolic process   4 terms 
  Biochemical function     catalytic activity     3 terms