Structure of PDB 2pp3 Chain B

Receptor sequence

>2pp3B (length=395)

SANSDAVTYAKAANTRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGR
QKPLTEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGE
DPNDIDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAK
LLGAHRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLAVGQPNC
AEDIRRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEE
PLDAYDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAP
RVGGISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWL
NPLFNEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP

3D structure

• PDB: 2pp3 Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.
• Chain: B
• Resolution: 2.2 Å

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	B	D226 E252 E278	D223 E249 E275
BS02	LGT	B	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

External links

• PDB: RCSB:2pp3, PDBe:2pp3, PDBj:2pp3
• PDBsum: 2pp3
• PubMed: 17649980
• UniProt: Q8ZL58|TAGAD_SALTY L-talarate/galactarate dehydratase (Gene Name=STM3697)