Structure of PDB 1jct Chain A

Receptor sequence
>1jctA (length=443) Species: 562 (Escherichia coli) [Search protein sequence]
QFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVG
EIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQT
FDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFF
VGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFND
FKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLK
GSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLS
LQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSLNHFDISLAMFTH
VAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEID
MDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
3D structure
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.
ChainA
Resolution2.75 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 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.
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 A D235 E260 N289 D232 E257 N286
BS02 GKR A N27 H32 T103 Y150 F152 K207 D235 N289 S340 R422 N24 H29 T100 Y147 F149 K204 D232 N286 S337 R419
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
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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