PDBsum entry: 1phq

Transferase

PDB id: 1phq

Contents

Protein chain

272 a.a. *

Ligands

FPE

Waters ×34

* Residue conservation analysis

PDB id:

1phq

Name:

Transferase

Title:

Crystal structure of kdo8p synthase in its binary complex wi substrate analog e-fpep

Structure:

2-dehydro-3-deoxyphosphooctonate aldolase. Chain: a. Synonym: phospho-2-dehydro-3-deoxyoctonate aldolase, 3-deox octulosonic acid 8-phosphate synthetase, kdo-8-phosphate sy kdo 8-p synthase. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: kdsa. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.70Å R-factor: 0.235 R-free: 0.322

Authors:

R.Vainer,N.Adir,T.Baasov,V.Belakhov,E.Rabkin

Key ref:

R.Vainer et al. Crystallographic analysis of the phosphoenol pyruvate binding site in e. Coli kdo8p synthase. To be published,

Date:

29-May-03 Release date: 13-Jul-04

Protein chain

P0A715  (KDSA_ECOLI) -  2-dehydro-3-deoxyphosphooctonate aldolase

Seq: 284 a.a.

Struc: 272 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.55 - 3-deoxy-8-phosphooctulonate synthase.
• Reaction: Phosphoenolpyruvate + D-arabinose 5-phosphate + H₂O = 2-dehydro-3- deoxy-D-octonate 8-phosphate + phosphate

Phosphoenolpyruvate (Bound ligand (Het Group name = FPE) matches with 90.91% similarity) + D-arabinose 5-phosphate + H(2)O = 2-dehydro-3- deoxy-D-octonate 8-phosphate + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: cytoplasm (2 terms)
• Biological process: metabolic process (3 terms)
• Biochemical function: catalytic activity (3 terms)