Structure of PDB 3ct2 Chain B Binding Site BS01

Receptor Information
>3ct2 Chain B (length=361) Species: 220664 (Pseudomonas protegens Pf-5) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HASAIESIETIIVDLPTINQTLVLIRLRCADGIEGLGESTTIGGLAYGNE
SPDSIKTNIDRFVAPLLIGQDASNINAAMLRLEQSIRGNTFAKSGIESAL
LDAQGKRLGLPVSELLGGRVRDALPVAWTLASGDTAKDIAEAQKMLDLRR
HRIFKLKIGAGEVDRDLAHVIAIKKALGDSASVRVDVNQAWDEAVALRAC
RILGGNGIDLIEQPISRNNRAGMVRLNASSPAPIMADESIECVEDAFNLA
REGAASVFALKIAKNGGPRATLRTAAIAEAAGIGLYGGTMLEGGIGTLAS
AHAFLTLNKLSWDTELFGPLLLTEDILAEPPVYRDFHLHVSKAPGLGLSL
DEERLAFFRRE
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3ct2 Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3ct2 Evolution of enzymatic activities in the enolase superfamily: stereochemically distinct mechanisms in two families of cis,cis-muconate lactonizing enzymes.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D200 E226 D251
Binding residue
(residue number reindexed from 1)		D186 E212 D237
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) T55 G58 T143 K169 K171 D200 N202 E226 D251 E252 S253 I254 K275 Y300 G302 T303 M304 H316 T328 E329 L330
Catalytic site (residue number reindexed from 1) T41 G44 T129 K155 K157 D186 N188 E212 D237 E238 S239 I240 K261 Y286 G288 T289 M290 H302 T314 E315 L316
Enzyme Commision number 5.5.1.1: muconate cycloisomerase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0016853 isomerase activity
GO:0018849 muconate cycloisomerase activity
GO:0018850 chloromuconate cycloisomerase activity
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0009056 catabolic process
GO:0009063 amino acid catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ct2, PDBe:3ct2, PDBj:3ct2
PDBsum3ct2
PubMed19220063
UniProtQ4K9X1

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