Structure of PDB 1jct Chain B Binding Site BS02

Receptor Information
>1jct Chain B (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
QSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSLNHFDISLAMFTHV
AAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM
DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
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 B Residue 502 [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 K207 D235 N289 S340 L341 H368 R422
Binding residue
(residue number reindexed from 1)		N23 H28 T99 Y146 K203 D231 N285 S336 L337 H364 R418
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) K201 K203 D231 N233 E256 N285 M286 D309 H335 L337 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:1jct, PDBe:1jct, PDBj:1jct
PDBsum1jct
PubMed11513584
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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