Structure of PDB 2pp1 Chain F Binding Site BS01

Receptor Information
>2pp1 Chain F (length=391) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SANSDAVTYAKRTAAETGDRIEWVKLSLAFLPLATPVSDAKVLTGRQKPL
TEVAIIIAEIRSRDGFEGVGFSYSKRAGGQGIYAHAKEIADNLLGEDPND
IDKIYTKLLWAGASVGRSGMAVQAISPIDIALWDMKAKRAGLPLAKLLGA
HRDSVQCYNTSGGFLHTPLDQVLKNVVISRENGIGGIKLKVGQPNCAEDI
RRLTAVREALGDEFPLMVDANQQWDRETAIRMGRKMEQFNLIWIEEPLDA
YDIEGHAQLAAALDTPIATGEMLTSFREHEQLILGNASDFVQPDAPRVGG
ISPFLKIMDLAAKHGRKLAPHFAMEVHLHLSAAYPLEPWLEHFEWLNPLF
NEQLELRDGRMWISDRHGLGFTLSEQARRWTQLTCEFGKRP
Ligand information
Ligand IDLLH
InChIInChI=1S/C5H9NO7/c7-1(3(9)5(11)12)2(8)4(10)6-13/h1-3,7-9,13H,(H,6,10)(H,11,12)/t1-,2+,3+/m0/s1
InChIKeyDMGBHBFPSRKPBV-ZVHKOUPVSA-N
SMILES
SoftwareSMILES
CACTVS 3.341ONC(=O)[CH](O)[CH](O)[CH](O)C(O)=O
CACTVS 3.341ONC(=O)[C@H](O)[C@H](O)[C@@H](O)C(O)=O
OpenEye OEToolkits 1.5.0[C@H]([C@H](C(=O)NO)O)([C@H](C(=O)O)O)O
ACDLabs 10.04O=C(O)C(O)C(O)C(O)C(=O)NO
OpenEye OEToolkits 1.5.0C(C(C(=O)NO)O)(C(C(=O)O)O)O
FormulaC5 H9 N O7
Name(2R,3S,4R)-2,3,4-TRIHYDROXY-5-(HYDROXYAMINO)-5-OXOPENTANOIC ACID
ChEMBL
DrugBank
ZINCZINC000002046851
PDB chain2pp1 Chain F Residue 806 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2pp1 Evolution of enzymatic activities in the enolase superfamily: L-talarate/galactarate dehydratase from Salmonella typhimurium LT2.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D46 K82 F171 K197 E278 H328 E348
Binding residue
(residue number reindexed from 1)		D39 K75 F164 K190 E271 H321 E341
Annotation score2
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.
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2pp1, PDBe:2pp1, PDBj:2pp1
PDBsum2pp1
PubMed17649980
UniProtQ8ZL58|TAGAD_SALTY L-talarate/galactarate dehydratase (Gene Name=STM3697)

[Back to BioLiP]