Structure of PDB 1g7v Chain A

Receptor sequence
>1g7vA (length=284) Species: 562 (Escherichia coli) [Search protein sequence]
MKQKVVSIGDINVANDLPFVLFGGMNVLESRDLAMRICEHYVTVTQKLGI
PYVFKASFDKANRSSIHSYRGPGLEEGMKIFQELKQTFGVKIITDVHEPS
QAQPVADVVDVIQLPAFLARQTDLVEAMAKTGAVINVKKPQFVSPGQMGN
IVDKFKEGGNEKVILCDRGANFGYDNLVVDMLGFSIMKKVSGNSPVIFDV
THALQCRDPFGAASGGRRAQVAELARAGMAVGLAGLFIEAHPDPEHAKCD
GPSALPLAKLEPFLKQMKAIDDLVKGFEELDTSK
3D structure
PDB1g7v Crystal structures of KDOP synthase in its binary complexes with the substrate phosphoenolpyruvate and with a mechanism-based inhibitor.
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N26 K60 D250
Catalytic site (residue number reindexed from 1) N26 K60 D250
Enzyme Commision number 2.5.1.55: 3-deoxy-8-phosphooctulonate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PAI A N62 R63 F117 R168 H202 Q205 A247 G251 P252 N62 R63 F117 R168 H202 Q205 A247 G251 P252 MOAD: Kd=0.4uM
PDBbind-CN: -logKd/Ki=6.40,Kd=0.4uM
Gene Ontology
Molecular Function
GO:0008676 3-deoxy-8-phosphooctulonate synthase activity
GO:0016740 transferase activity
GO:0042802 identical protein binding
Biological Process
GO:0009058 biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0019294 keto-3-deoxy-D-manno-octulosonic acid biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Cellular Component
External links
PDB RCSB:1g7v, PDBe:1g7v, PDBj:1g7v
PDBsum1g7v
PubMed11371194
UniProtP0A715|KDSA_ECOLI 2-dehydro-3-deoxyphosphooctonate aldolase (Gene Name=kdsA)

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