Structure of PDB 2nxi Chain G

Receptor sequence
>2nxiG (length=259) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
KFLVIAGMNAIESEELLLKVGEEIKRLSEKFKEVEFVFKSSFDKANRSSI
HSFRGHGLEYGVKALRKVKEEFGLKITTDIHESWQAEPVAEVADIIQIPA
FLCRQTDLLLAAAKTGRAVNVKKGQFLAPWDTKNVVEKLKFGGAKEIYLT
ERGTTFGYNNLVVDFRSLPIMKQWAKVIYDATHSVQLPGGLGDGMREFIF
PLIRAAVAVGCDGVFMETHPEPEKALSDASTQLPLSQLEGIIEAILEIRE
VASKYYETI
3D structure
PDB2nxi Structural and mechanistic changes along an engineered path from metallo to nonmetallo 3-deoxy-D-manno-octulosonate 8-phosphate synthases
ChainG
Resolution2.3 Å
3D
structure
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Enzymatic activity
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 PEP G K41 K46 D81 Q99 P101 K124 R154 H185 K39 K44 D79 Q97 P99 K122 R152 H183
BS02 PEP G R49 S50 D233 R47 S48 D228
Gene Ontology
Molecular Function
GO:0008676 3-deoxy-8-phosphooctulonate synthase activity
GO:0016740 transferase activity
Biological Process
GO:0009058 biosynthetic process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0019294 keto-3-deoxy-D-manno-octulosonic acid biosynthetic process
GO:0046364 monosaccharide biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2nxi, PDBe:2nxi, PDBj:2nxi
PDBsum2nxi
PubMed17381075
UniProtO66496|KDSA_AQUAE 2-dehydro-3-deoxyphosphooctonate aldolase (Gene Name=kdsA)

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