Structure of PDB 1ec9 Chain C

Receptor sequence
>1ec9C (length=443) Species: 562 (Escherichia coli) [Search protein sequence]
QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVG
EIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQT
FDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFF
VGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND
FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLK
GSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLS
LQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTH
VAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID
MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
3D structure
PDB1ec9 Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli.
ChainC
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 MG C D235 E260 N289 D232 E257 N286
BS02 XYH C H32 T103 Y150 F152 K207 D235 N237 N289 H339 S340 H368 H29 T100 Y147 F149 K204 D232 N234 N286 H336 S337 H365 MOAD: Ki=0.8mM
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

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Molecular Function
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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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