Structure of PDB 1ec9 Chain A Binding Site BS02

Receptor Information
>1ec9 Chain A (length=443) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVG
EIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQT
FDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFF
VGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND
FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLK
GSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLS
LQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTH
VAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID
MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
Ligand information
Ligand IDXYH
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)/p-1/t1-,2-,3+/m0/s1
InChIKeyDMGBHBFPSRKPBV-XZIMBLGRSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(NO)C(O)C(O)C(O)C([O-])=O
OpenEye OEToolkits 1.5.0[C@H]([C@@H](C(=O)NO)O)([C@H](C(=O)[O-])O)O
CACTVS 3.341ONC(=O)[CH](O)[CH](O)[CH](O)C([O-])=O
OpenEye OEToolkits 1.5.0C(C(C(=O)NO)O)(C(C(=O)[O-])O)O
CACTVS 3.341ONC(=O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O
FormulaC5 H8 N O7
NameXYLAROHYDROXAMATE
ChEMBL
DrugBankDB03734
ZINC
PDB chain1ec9 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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PDB1ec9 Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		H32 T103 Y150 K207 D235 N237 N289 H339 S340 N341 H368 R422
Binding residue
(residue number reindexed from 1)		H29 T100 Y147 K204 D232 N234 N286 H336 S337 N338 H365 R419
Annotation score3
Binding affinityMOAD: Ki=0.8mM
PDBbind-CN: -logKd/Ki=3.10,Ki=0.8mM
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) K202 K204 D232 N234 E257 N286 M287 D310 H336 N338 I362
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:1ec9, PDBe:1ec9, PDBj:1ec9
PDBsum1ec9
PubMed10769114
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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