Structure of PDB 1w2t Chain B Binding Site BS01

Receptor Information
>1w2t Chain B (length=432) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LFKPNYHFFPITGWMNDPNGLIFWKGKYHMFYQYNPRKPEWGNICWGHAV
SDDLVHWRHLPVALYPDDETHGVFSGSAVEKDGKMFLVYTYYRDPTHNKG
EKETQCVVMSENGLDFVKYDGNPVISKPPEEGTHAFRDPKVNRSNGEWRM
VLGSGKDEKIGRVLLYTSDDLFHWKYEGAIFEDETTKEIDCPDLVRIGEK
DILIYSITSTNSVLFSMGELKEGKLNVEKRGLLDHGTDFYAAQTFFGTDR
VVVIGWLQSWLRTGLYPTKREGWNGVMSLPRELYVENNELKVKPVDELLA
LRKRKVFETAKSGTFLLDVKENSYEIVCEFSGEIELRMGNESEEVVITKS
RDELIVDTTRSGVSGGEVRKSTVEDEATNRIRAFLDSCSVEFFFNDSIAF
SFRIHPENVYNILSVKSNQVKLEVFELENIWL
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain1w2t Chain H Residue 1 [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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PDB1w2t Crystal Structure of Inactivated Thermotoga Maritima Invertase in Complex with the Trisaccharide Substrate Raffinose.
Resolution1.87 Å
Binding residue
(original residue number in PDB)		R137 T208 W260
Binding residue
(residue number reindexed from 1)		R137 T208 W260
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D17 D190
Catalytic site (residue number reindexed from 1) D17 D190
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004564 beta-fructofuranosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1w2t, PDBe:1w2t, PDBj:1w2t
PDBsum1w2t
PubMed16411890
UniProtO33833|BFRA_THEMA Beta-fructosidase (Gene Name=bfrA)

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