Structure of PDB 3d47 Chain E

Receptor sequence
>3d47E (length=405) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
MENIMTLPKIKHVRAWFIGGATAEKGAGGGDYHDQGGNHWIDDHIATPMS
KYRDYEQSRQSFGINVLGTLIVEVEAENRQTGFAVSTAGEMGCFIVEKHL
NRFIEGKCVSDIKLIHDQMLGATMYYSGSGGLVMNTISCVDLALWDLFGK
VVGLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGD
AGIRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKW
IEECLPPQQYEGYRELKRNAPAGMMVTSGEHHGTLQSFRTLAETGIDIMQ
PDVGWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEF
LMTSPDCSTLRPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCHLK
RPYSH
3D structure
PDB3d47 Crystal structure of L-rhamnonate dehydratase from Salmonella typhimurium complexed with Mg and D-malate.
ChainE
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K189 P191 G195 H197 A201 D226 W228 E252 T277 E280 Q300 D302 H329 E349 P362
Catalytic site (residue number reindexed from 1) K189 P191 G195 H197 A201 D226 W228 E252 T277 E280 Q300 D302 H329 E349 P362
Enzyme Commision number 4.2.1.90: L-rhamnonate 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 E D226 E252 E280 D226 E252 E280
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016829 lyase activity
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0050032 L-rhamnonate dehydratase activity
Biological Process
GO:0009063 amino acid catabolic process
GO:0016052 carbohydrate catabolic process

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Molecular Function

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Biological Process
External links
PDB RCSB:3d47, PDBe:3d47, PDBj:3d47
PDBsum3d47
PubMed
UniProtQ8ZNF9|RHMD_SALTY L-rhamnonate dehydratase (Gene Name=rhmD)

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