Structure of PDB 1ecq Chain A

Receptor sequence
>1ecqA (length=444) Species: 562 (Escherichia coli) [Search protein sequence]
SQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGV
GEIPGGEKIRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQ
TFDLRTTIHVVTGIEAAMLDLLGQHLGVNVASLLGDGQQRSEVEMLGYLF
FVGNRKATPLPYQSQPDDSCDWYRLRHEEAMTPDAVVRLAEAAYEKYGFN
DFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAWSLNEAIKIGKYL
KGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGHTL
SLQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFT
HVAAAAPGKITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEI
DMDQVMKAHELYQKHGLGARDDAMGMQYLIPGWTFDNKRPCMVR
3D structure
PDB1ecq Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by 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 N341 I365
Catalytic site (residue number reindexed from 1) K203 K205 D233 N235 E258 N287 M288 D311 H337 N339 I363
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 DXG A N27 H32 T103 Y150 F152 K207 D235 N237 N289 H339 S340 N341 H368 R422 N25 H30 T101 Y148 F150 K205 D233 N235 N287 H337 S338 N339 H366 R420 MOAD: Ki=1mM
PDBbind-CN: -logKd/Ki=3.00,Ki=1.0mM
BS02 MG A D235 E260 N289 D233 E258 N287
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:1ecq, PDBe:1ecq, PDBj:1ecq
PDBsum1ecq
PubMed10769114
UniProtP0AES2|GUDD_ECOLI Glucarate dehydratase (Gene Name=gudD)

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