Structure of PDB 1ec9 Chain B Binding Site BS02
Receptor Information
>1ec9 Chain B (length=443) Species:
562
(Escherichia coli) [
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QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVG
EIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQT
FDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFF
VGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND
FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLK
GSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLS
LQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTH
VAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID
MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
Ligand information
Ligand ID
XYH
InChI
InChI=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
InChIKey
DMGBHBFPSRKPBV-XZIMBLGRSA-M
SMILES
Software
SMILES
ACDLabs 10.04
O=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 3.341
ONC(=O)[CH](O)[CH](O)[CH](O)C([O-])=O
OpenEye OEToolkits 1.5.0
C(C(C(=O)NO)O)(C(C(=O)[O-])O)O
CACTVS 3.341
ONC(=O)[C@@H](O)[C@H](O)[C@@H](O)C([O-])=O
Formula
C5 H8 N O7
Name
XYLAROHYDROXAMATE
ChEMBL
DrugBank
DB03734
ZINC
PDB chain
1ec9 Chain B Residue 500 [
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Receptor-Ligand Complex Structure
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PDB
1ec9
Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
N27 H32 T103 Y150 F152 K207 D235 N237 N289 H339 S340 N341 H368 R422
Binding residue
(residue number reindexed from 1)
N24 H29 T100 Y147 F149 K204 D232 N234 N286 H336 S337 N338 H365 R419
Annotation score
3
Binding affinity
MOAD
: 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
PDBsum
1ec9
PubMed
10769114
UniProt
P0AES2
|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)
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