Structure of PDB 3rra Chain A

Receptor sequence
>3rraA (length=374) Species: 402626 (Ralstonia pickettii 12J) [Search protein sequence]
VKITRLTTYRLPPRWMFLKVETDEGVTGWGEPVIEGRARTVEAAVHELSD
YLIGQDPSRINDLWQTMYRAGFYRGGPILMSAIAGIDQALWDIKGKVLGV
PVYELLGGLVRDKMRTYSWVGGDRPADVIAGMKALQAGGFDHFKLNGCEE
MGIIDTSRAVDAAVARVAEIRSAFGNTVEFGLDFHGRVSAPMAKVLIKEL
EPYRPLFIEEPVLAEQAETYARLAAHTHLPIAAGERMFSRFDFKRVLEAG
GVSILQPDLSHAGGITECVKIAAMAEAYDVALAPHCPLGPIALAACLHVD
FVSWNATLQEQSMELLDYVRNKADFALEGGYIRPPRLPGLGVDIDEALVI
ERSKEAPNPVWRHADGSVAEWAEN
3D structure
PDB3rra Crystal structure of enolase PRK14017 from Ralstonia pickettii
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I34 R37 Y117 K144 N146 E150 D183 H185 E209 G234 E235 R236 Q256 D258 H285 P287 E310
Catalytic site (residue number reindexed from 1) I34 R37 Y117 K144 N146 E150 D183 H185 E209 G234 E235 R236 Q256 D258 H285 P287 E310
Enzyme Commision number 4.2.1.6: galactonate dehydratase.
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 MG A D183 E209 E235 D183 E209 E235
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008869 galactonate dehydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0009063 amino acid catabolic process
GO:0034194 D-galactonate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3rra, PDBe:3rra, PDBj:3rra
PDBsum3rra
PubMed
UniProtB2UCA8|DGOD_RALPJ D-galactonate dehydratase (Gene Name=dgoD)

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