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Structure of PDB 2pwg Chain B Binding Site BS02

Receptor Information
>2pwg Chain B (length=556) Species: 265293 (Burkholderia ubonensis subsp. mesacidophila) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PGAPWWKSAVFYQVYPRSFKDTNGDGIGDFKGLTEKLDYLKGLGIDAIWI
NPHYASPNTDNGYDISDYREVMKEYGTMEDFDRLMAELKKRGMRLMVDVV
INHSSDQHEWFKSSRASKDNPYRDYYFWRDGKDGHEPNNYPSFFGGSAWE
KDPVTGQYYLHYFGRQQPDLNWDTPKLREELYAMLRFWLDKGVSGMRFDT
VATYSKTPGFPDLTPEQMKNFAEAYTQGPNLHRYLQEMHEKVFDHYDAVT
AGEIFGAPLNQVPLFIDSRRKELDMAFTFDLIRYDRALDRWHTIPRTLAD
FRQTIDKVDAIAGEYGWNTFFLGNHDNPRAVSHFGDDRPQWREASAKALA
TVTLTQRGTPFIFQGDELGMTNYPFKTLQDFDDIEVKGFFQDYVETGKAT
AEELLTNVALTSRDNARTPFQWDDSANAGFTTGKPWLKVNPNYTEINAAR
EIGDPKSVYSFYRNLISIRHETPALSTGSYRDIDPSNADVYAYTRSQDGE
TYLVVVNFKAEPRSFTLPDGMHIAETLIESSSPAAPAAGAASLELQPWQS
GIYKVK
Ligand information
Ligand IDCTS
InChIInChI=1S/C8H15NO4/c10-4-1-2-9-3-5(11)7(12)8(13)6(4)9/h4-8,10-13H,1-3H2/t4-,5-,6+,7+,8+/m0/s1
InChIKeyJDVVGAQPNNXQDW-TVNFTVLESA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[C@H]1CCN2C[C@H](O)[C@@H](O)[C@H](O)[C@@H]12
OpenEye OEToolkits 1.5.0C1CN2CC(C(C(C2C1O)O)O)O
OpenEye OEToolkits 1.5.0C1C[N@]2C[C@@H]([C@H]([C@@H]([C@H]2[C@H]1O)O)O)O
CACTVS 3.341O[CH]1CCN2C[CH](O)[CH](O)[CH](O)[CH]12
ACDLabs 10.04OC1CCN2C1C(O)C(O)C(O)C2
FormulaC8 H15 N O4
NameCASTANOSPERMINE;
(1S,6S,7R,8R,8AR)-1,6,7,8-TETRAHYDROXYINDOLIZIDINE
ChEMBLCHEMBL311226
DrugBankDB01816
ZINCZINC000003775177
PDB chain2pwg Chain B Residue 8001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2pwg Trehalulose synthase native and carbohydrate complexed structures provide insights into sucrose isomerization.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		D61 Y64 H104 F164 D200 E254 D327 R414
Binding residue
(residue number reindexed from 1)		D60 Y63 H103 F163 D199 E253 D326 R413
Annotation score1
Binding affinityMOAD: Ki=15uM
Enzymatic activity
Catalytic site (original residue number in PDB) D99 R198 D200 E254 H326 D327
Catalytic site (residue number reindexed from 1) D98 R197 D199 E253 H325 D326
Enzyme Commision number 5.4.99.11: isomaltulose synthase.
Gene Ontology
Molecular Function
GO:0004556 alpha-amylase activity
GO:0016853 isomerase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009313 oligosaccharide catabolic process

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Molecular Function
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Biological Process
External links

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