Structure of PDB 3cxo Chain B

Receptor sequence
>3cxoB (length=402) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2) [Search protein sequence]
IMTLPKIKHVRAWFIGGATAEKGAGGGDYHDQGGNHWIDDHIATPMSKYR
DYEQSRQSFGINVLGTLIVEVEAENRQTGFAVSTAGEMGCFIVEKHLNRF
IEGKCVSDIKLIHDQMLGATMYYSGSGGLVMNTISCVDLALWDLFGKVVG
LPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAGI
RKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIEE
CLPPQQYEGYRELKRNAPAGMMVTSGEHHGTLQSFRTLAETGIDIMQPDV
GWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLMT
SPDCSTLRPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCHLKRPY
SH
3D structure
PDB3cxo Evolution of enzymatic activities in the enolase superfamily: L-rhamnonate dehydratase.
ChainB
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) Y55 K189 P191 G195 H197 A201 D226 W228 E252 T277 G279 E280 Q300 D302 H329 E349 S354
Catalytic site (residue number reindexed from 1) Y52 K186 P188 G192 H194 A198 D223 W225 E249 T274 G276 E277 Q297 D299 H326 E346 S351
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 B D226 E252 E280 D223 E249 E277
BS02 1N5 B H33 I45 R59 K189 P191 D226 W228 E280 H329 E349 H30 I42 R56 K186 P188 D223 W225 E277 H326 E346
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:3cxo, PDBe:3cxo, PDBj:3cxo
PDBsum3cxo
PubMed18754693
UniProtQ8ZNF9|RHMD_SALTY L-rhamnonate dehydratase (Gene Name=rhmD)

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