Structure of PDB 6lgg Chain B Binding Site BS02

Receptor Information
>6lgg Chain B (length=569) Species: 7091 (Bombyx mori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPTEVIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGV
DAIWMSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKV
LLDFVPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSN
WVSQFGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWL
DKGADGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLY
TKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSQGYANVSMTMLYYGNE
DGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGN
HDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTV
DIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQ
EINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRS
LPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEIT
SSQLSLEAGEALVLKAQPI
Ligand information
Ligand IDFRU
InChIInChI=1S/C6H12O6/c7-1-3-4(9)5(10)6(11,2-8)12-3/h3-5,7-11H,1-2H2/t3-,4-,5+,6-/m1/s1
InChIKeyRFSUNEUAIZKAJO-ARQDHWQXSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04OC1C(O)C(OC1(O)CO)CO
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@](O1)(CO)O)O)O)O
CACTVS 3.341OC[CH]1O[C](O)(CO)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C(C1C(C(C(O1)(CO)O)O)O)O
CACTVS 3.341OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O
FormulaC6 H12 O6
Namebeta-D-fructofuranose;
beta-D-fructose;
D-fructose;
fructose
ChEMBLCHEMBL604608
DrugBank
ZINCZINC000001529270
PDB chain6lgg Chain F Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6lgg Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.84 Å
Binding residue
(original residue number in PDB)		A248 Q322 Y324 D389 E440
Binding residue
(residue number reindexed from 1)		A211 Q285 Y287 D352 E403
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 Q322 H388 D389
Catalytic site (residue number reindexed from 1) D103 D210 Q285 H351 D352
Enzyme Commision number 3.2.1.20: alpha-glucosidase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6lgg, PDBe:6lgg, PDBj:6lgg
PDBsum6lgg
PubMed32381508
UniProtA0A077JI83

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