Structure of PDB 2nxi Chain I

Receptor sequence
>2nxiI (length=262) Species: 63363 (Aquifex aeolicus) [Search protein sequence]
KFLVIAGMNAIESEELLLKVGEEIKRLSEKFKEVEFVFKSSFDKANRSSI
HSFRGHGLEYGVKALRKVKEEFGLKITTDIHESWQAEPVAEVADIIQIPA
FLCRQTDLLLAAAKTGRAVNVKKGQFLAPWDTKNVVEKLKFGGAKEIYLT
ERGTTFGYNNLVVDFRSLPIMKQWAKVIYDATHSVQLPGGLGDKSGGMRE
FIFPLIRAAVAVGCDGVFMETHPEPEKALSDASTQLPLSQLEGIIEAILE
IREVASKYYETI
3D structure
PDB2nxi Structural and mechanistic changes along an engineered path from metallo to nonmetallo 3-deoxy-D-manno-octulosonate 8-phosphate synthases
ChainI
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 I K41 Q99 P101 A102 K124 R154 H185 K39 Q97 P99 A100 K122 R152 H183
BS02 PEP I R49 S50 K196 S197 R47 S48 K194 S195
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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