Structure of PDB 6s2b Chain A Binding Site BS01

Receptor Information
>6s2b Chain A (length=512) Species: 27300 (Schwanniomyces occidentalis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SIDLSVDTSEYNRPLIHFTPEKGWMNAPNGLFYDKTAKLWHLYFQYNPNA
TAWGQPLYWGHATSNDLVHWDEHEIAIGPEHDNEGIFSGSIVVDHNNTSG
FFNSSIDPNQRIVAIYTNNIPDNQTQDIAFSLDGGYTFTKYENNPVIDVS
SNQFRDPKVFWHEDSNQWIMVVSKSQEYKIQIFGSANLKNWVLNSNFSSG
YYGNQYECPGLIEVPIENSDKSKWVMFLAINPGSPLGGSINQYFVGDFDG
FQFVPDDSQTRFVDIGKDFYAFQTFSEVEHGVLGLAWASNWQYADQVPTN
PWRSSTSLARNYTLRYVHTNAETKQLTLIQNPVLPDSINVVDKLKKKNVK
LTNKKPIKTNFKGSTGLFDFNITFKVLNLNVSPGKTHFDILINSQELNSS
VDSIKIGFDSSQSSFYIDRHIPNVEFPRKQFFTDKLAAYLEPLDYDQDLR
VFSLYGIVDKNIIELYFNDGTVAMTNTFFMGEGKYPHDIQIVTDTEEPLF
ELESVIIRELNK
Ligand information
Ligand IDKTE
InChIInChI=1S/C10H20O9/c11-1-5(14)6(15)3-18-10(4-13)9(17)8(16)7(2-12)19-10/h5-9,11-17H,1-4H2/t5-,6+,7+,8+,9-,10+/m0/s1
InChIKeyCPODZCVBMHISBV-NSTDSTDXSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7C(C1C(C(C(O1)(CO)OCC(C(CO)O)O)O)O)O
OpenEye OEToolkits 2.0.7C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)OC[C@H]([C@H](CO)O)O)O)O)O
CACTVS 3.385OC[CH](O)[CH](O)CO[C]1(CO)O[CH](CO)[CH](O)[CH]1O
CACTVS 3.385OC[C@H](O)[C@H](O)CO[C@]1(CO)O[C@H](CO)[C@@H](O)[C@@H]1O
FormulaC10 H20 O9
Name(2~{S},3~{R})-4-[(2~{R},3~{S},4~{S},5~{R})-2,5-bis(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]oxybutane-1,2,3-triol
ChEMBL
DrugBank
ZINC
PDB chain6s2b Chain A Residue 608 [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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PDB6s2b New insights into the molecular mechanism behind mannitol and erythritol fructosylation by beta-fructofuranosidase from Schwanniomyces occidentalis.
Resolution1.88 Å
Binding residue
(original residue number in PDB)		N49 Q68 W76 F110 S111 R178 D179 E230 Y293 W314
Binding residue
(residue number reindexed from 1)		N26 Q45 W53 F87 S88 R155 D156 E207 Y270 W291
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) A50 E230
Catalytic site (residue number reindexed from 1) A27 E207
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6s2b, PDBe:6s2b, PDBj:6s2b
PDBsum6s2b
PubMed33785821
UniProtE5D0X5

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