Structure of PDB 1jct Chain A Binding Site BS02

Receptor Information
>1jct 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
LQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSLNHFDISLAMFTH
VAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID
MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
Ligand information
Ligand IDGKR
InChIInChI=1S/C6H10O8/c7-1(3(9)5(11)12)2(8)4(10)6(13)14/h1-4,7-10H,(H,11,12)(H,13,14)/p-2/t1-,2-,3-,4+/m0/s1
InChIKeyDSLZVSRJTYRBFB-LLEIAEIESA-L
SMILES
SoftwareSMILES
CACTVS 3.341O[C@@H]([C@H](O)[C@H](O)C([O-])=O)[C@@H](O)C([O-])=O
OpenEye OEToolkits 1.5.0[C@H]([C@@H]([C@@H](C(=O)[O-])O)O)([C@H](C(=O)[O-])O)O
ACDLabs 10.04[O-]C(=O)C(O)C(O)C(O)C(O)C([O-])=O
OpenEye OEToolkits 1.5.0C(C(C(C(=O)[O-])O)O)(C(C(=O)[O-])O)O
CACTVS 3.341O[CH]([CH](O)[CH](O)C([O-])=O)[CH](O)C([O-])=O
FormulaC6 H8 O8
NameD-GLUCARATE
ChEMBL
DrugBank
ZINC
PDB chain1jct 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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PDB1jct Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		N27 H32 T103 Y150 F152 K207 D235 N289 S340 R422
Binding residue
(residue number reindexed from 1)		N24 H29 T100 Y147 F149 K204 D232 N286 S337 R419
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K205 K207 D235 N237 E260 N289 M290 D313 H339 L341 I365
Catalytic site (residue number reindexed from 1) K202 K204 D232 N234 E257 N286 M287 D310 H336 L338 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:1jct, PDBe:1jct, PDBj:1jct
PDBsum1jct
PubMed11513584
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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