Structure of PDB 3stp Chain A

Receptor sequence
>3stpA (length=390) Species: 384765 (Roseibium aggregatum IAM 12614) [Search protein sequence]
MKIKSVRTRVWTWKGPTVPPQGNFCTNASDALWMKGDAMSSFRFHQWLTC
EVETEDGTIGIGNAALAPSVVKKVIDDWYAPLVIGEDPFDYAYIWEKMYR
RSHAWGRKGIGMTAISAIDIAIWDLMGKLVGKPVFKLLGGRTKDRIPVYY
SKLYAGSIEAMQKEAEEAMKGGYKAFKSRFGYGPKDGMPGMRENLKRVEA
VREVIGYDNDLMLECYMGWNLDYAKRMLPKLAPYEPRWLEEPVIADDVAG
YAELNAMNIVPISGGEHEFSVIGCAELINRKAVSVLQYDTNRVGGITAAQ
KINAIAEAAQIPVIPHAGQMHNYHLTMANTNCPISEYFPVFDVEVGNELF
YYIFEGDPEAVDGYLQLDDDLPGLGIAISDKHLQHFDITE
3D structure
PDB3stp Crystal structure of a putative galactonate dehydratase
ChainA
Resolution1.88 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L66 S69 S151 K177 R179 P189 E214 Y216 E240 G265 E266 H267 Q287 D289 I311 H316 E336 F341
Catalytic site (residue number reindexed from 1) L66 S69 S151 K177 R179 P189 E214 Y216 E240 G265 E266 H267 Q287 D289 I311 H316 E336 F341
Enzyme Commision number ?
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 E214 E240 E266 E214 E240 E266
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016836 hydro-lyase activity
GO:0046872 metal ion binding
GO:0050032 L-rhamnonate dehydratase activity
Biological Process
GO:0016052 carbohydrate catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3stp, PDBe:3stp, PDBj:3stp
PDBsum3stp
PubMed
UniProtA0NP48

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