Structure of PDB 2pp1 Chain C

Receptor sequence

>2pp1C (length=391)

SANSDAVTYAKRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGRQKPL
TEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPND
IDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGA
HRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDI
RRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDA
YDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAPRVGG
ISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLF
NEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP

3D structure

• PDB: 2pp1 Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.
• Chain: C
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K48 S81 K195 K197 D226 N228 E252 G277 E278 D301 H328 E348
• Catalytic site (residue number reindexed from 1): K41 S74 K188 K190 D219 N221 E245 G270 E271 D294 H321 E341
• 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	LLH	C	D46 K48 K82 F171 K197 E278 H328 E348	D39 K41 K75 F164 K190 E271 H321 E341

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:2pp1, PDBe:2pp1, PDBj:2pp1
• PDBsum: 2pp1
• PubMed: 17649980
• UniProt: Q8ZL58|TAGAD_SALTY L-talarate/galactarate dehydratase (Gene Name=STM3697)