Structure of PDB 2pp3 Chain A

Receptor sequence
>2pp3A (length=395) [Search protein sequence]
SANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGR
QKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGE
DPNDIDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAK
LLGAHRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLAVGQPNC
AEDIRRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEE
PLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAP
RVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWL
NPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
3D structure
PDB2pp3 Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 S81 K195 A197 D226 N228 E252 G277 E278 D301 H328 E348
Catalytic site (residue number reindexed from 1) K45 S78 K192 A194 D223 N225 E249 G274 E275 D298 H325 E345
Enzyme Commision number 4.2.1.156: L-talarate dehydratase.
4.2.1.42: galactarate 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 D226 E252 E278 D223 E249 E275
BS02 LGT A D46 K82 K195 D226 N228 E278 H328 E348 F350 D43 K79 K192 D223 N225 E275 H325 E345 F347
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008867 galactarate dehydratase activity
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:1990594 L-altrarate dehydratase activity
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process
GO:0046392 galactarate catabolic process
GO:1903663 L-altrarate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2pp3, PDBe:2pp3, PDBj:2pp3
PDBsum2pp3
PubMed17649980
UniProtQ8ZL58|TAGAD_SALTY L-talarate/galactarate dehydratase (Gene Name=STM3697)

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