Structure of PDB 1ec8 Chain A Binding Site BS02

Receptor Information
>1ec8 Chain A (length=442) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGE
IPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTF
DLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFV
GNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDF
KLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLKG
SLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSL
QSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHV
AAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM
DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
Ligand information
Ligand IDGLR
InChIInChI=1S/C6H8O7/c7-2(4(9)6(12)13)1-3(8)5(10)11/h2,4,7,9H,1H2,(H,10,11)(H,12,13)/p-2/t2-,4+/m0/s1
InChIKeyQUURPCHWPQNNGL-ZAFYKAAXSA-L
SMILES
SoftwareSMILES
CACTVS 3.341O[CH](CC(=O)C([O-])=O)[CH](O)C([O-])=O
OpenEye OEToolkits 1.5.0C([C@@H]([C@H](C(=O)[O-])O)O)C(=O)C(=O)[O-]
OpenEye OEToolkits 1.5.0C(C(C(C(=O)[O-])O)O)C(=O)C(=O)[O-]
CACTVS 3.341O[C@@H](CC(=O)C([O-])=O)[C@@H](O)C([O-])=O
ACDLabs 10.04O=C([O-])C(O)C(O)CC(=O)C([O-])=O
FormulaC6 H6 O7
Name2,3-DIHYDROXY-5-OXO-HEXANEDIOATE
ChEMBL
DrugBankDB03237
ZINC
PDB chain1ec8 Chain A Residue 499 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ec8 Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		N27 H32 T103 Y150 K207 D235 N237 N289 H339 S340 N341 H368 R422
Binding residue
(residue number reindexed from 1)		N23 H28 T99 Y146 K203 D231 N233 N285 H335 S336 N337 H364 R418
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K205 K207 D235 N237 E260 N289 M290 D313 H339 N341 I365
Catalytic site (residue number reindexed from 1) K201 K203 D231 N233 E256 N285 M286 D309 H335 N337 I361
Enzyme Commision number 4.2.1.40: glucarate dehydratase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0008872 glucarate dehydratase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0019394 glucarate catabolic process
GO:0042838 D-glucarate catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ec8, PDBe:1ec8, PDBj:1ec8
PDBsum1ec8
PubMed10769114
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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