Structure of PDB 1jdf Chain A

Receptor sequence
>1jdfA (length=442) Species: 562 (Escherichia coli) [Search protein sequence]
FTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGE
IPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTF
DLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFV
GNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFNDF
KLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYLKG
SLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTLSL
QSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSDNHFDISLAMFTHV
AAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDM
DQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
3D structure
PDB1jdf 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
Resolution2.0 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 D341 I365
Catalytic site (residue number reindexed from 1) K201 K203 D231 N233 E256 N285 M286 D309 H335 D337 I361
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 D231 E256 N285
BS02 GLR A N27 H32 T103 Y150 F152 K207 D235 E260 N289 H339 D341 H368 R422 N23 H28 T99 Y146 F148 K203 D231 E256 N285 H335 D337 H364 R418
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:1jdf, PDBe:1jdf, PDBj:1jdf
PDBsum1jdf
PubMed11513584
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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