Structure of PDB 2gsh Chain B

Receptor sequence

>2gshB (length=403) Species: 99287 (Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)

NIMTLPKIKHVRAWFIGGATAEKGAGGGDYHDQGGNHWIDDHIATPMSKY
RDYEQSRQSFGINVLGTLIVEVEAENRQTGFAVSTAGEMGCFIVEKHLNR
FIEGKCVSDIKLIHDQMLGATMYYSGSGGLVMNTISCVDLALWDLFGKVV
GLPVYKLLGGAVRDEIQFYATGARPDLAKEMGFIGGKMPTHWGPHDGDAG
IRKDAAMVADMREKCGPDFWLMLDCWMSQDVNYATKLAHACAPFNLKWIE
ECLPPQQYEGYRELKRNAPAGMMVTSGEHHGTLQSFRTLAETGIDIMQPD
VGWCGGLTTLVEIAALAKSRGQLVVPHGSSVYSHHAVITFTNTPFSEFLM
TSPDCSTLRPQFDPILLDEPVPVNGRIHKSVLDKPGFGVELNRDCHLKRP
YSH

3D structure

• PDB: 2gsh Crystal Structure of L-rhamnonate dehydratase from Salmonella Typhimurium Lt2
• Chain: B
• Resolution: 2.393 Å

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): Y53 K187 P189 G193 H195 A199 D224 W226 E250 T275 G277 E278 Q298 D300 H327 E347 S352
• 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	D224 E250 E278

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

External links

• PDB: RCSB:2gsh, PDBe:2gsh, PDBj:2gsh
• PDBsum: 2gsh
• UniProt: Q8ZNF9|RHMD_SALTY L-rhamnonate dehydratase (Gene Name=rhmD)