Structure of PDB 3twb Chain A

Receptor sequence
>3twbA (length=415) Species: 550537 (Salmonella enterica subsp. enterica serovar Enteritidis str. P125109) [Search protein sequence]
NLKITNVKTILTAPGGIDLAVVKIETNEPGLYGLGCATFTQRIFAVKSAI
DEYMAPFLVGKDPTRIEDIWQSGVVSGYWRNGPIMNNALSGVDMALWDIK
GKLAGMPVYDLLGGKCRDGIPLYCHTDGGDEVEVEDNIRARMEEGYQYVR
CQMGMYGGAGTDDLKLIATQLARAKNIQPKRSPRSKTPGIYFDPDAYAKS
VPRLFDHLRNKLGFGIEFIHDVHERVTPVTAINLAKTLEQYQLFYLEDPV
APENIDWLKMLRQQSSTPISMGELFVNVNEWKPLIDNRLIDYIRCHVSTI
GGITPARKLAVYSELNGVRTAWHGPGDISPVGVCANMHLDLSSPNFGIQE
YTPMNDALRDVFPGCPEIDHGYAYLNDKPGLGIDIDEAKAAKYPCEGGIP
SWTMARTPDGTASRP
3D structure
PDB3twb Crystal Structure of Gluconate Dehydratase from Salmonella Enterica P125109
ChainA
Resolution1.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) F43 R46 P125 R154 Q156 D166 D225 H227 E251 G276 E277 L278 R298 H300 H327 P329 E354 P419
Catalytic site (residue number reindexed from 1) F39 R42 P121 R150 Q152 D162 D221 H223 E247 G272 E273 L274 R294 H296 H323 P325 E350 P415
Enzyme Commision number 4.2.1.-
4.2.1.39: gluconate 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 D225 E251 E277 D221 E247 E273
BS02 GCO A R154 Y160 D225 H227 E277 H327 P329 D331 E354 R150 Y156 D221 H223 E273 H323 P325 D327 E350
BS03 GCO A Y82 W83 Y78 W79
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
GO:0047929 gluconate 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:3twb, PDBe:3twb, PDBj:3twb
PDBsum3twb
PubMed
UniProtB5R541|DGD_SALEP D-galactonate dehydratase family member SEN1436 (Gene Name=SEN1436)

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