Structure of PDB 6lgi Chain A Binding Site BS04

Receptor Information
>6lgi Chain A (length=570) Species: 7091 (Bombyx mori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PPPTEVIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAG
VDAIWMSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLK
VLLDFVPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPS
NWVSQFGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFW
LDKGADGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPL
YTKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSQGYANVSMTMLYYGN
EDGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFG
NHDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDT
VDIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDY
QEINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVR
SLPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEI
TSSQLSLEAGEALVLKAQPI
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 chain6lgi Chain A Residue 705 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6lgi Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.6 Å
Binding residue
(original residue number in PDB)
Q322 Y324 D389 E440
Binding residue
(residue number reindexed from 1)
Q286 Y288 D353 E404
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 Q322 H388 D389
Catalytic site (residue number reindexed from 1) D104 D211 Q286 H352 D353
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

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Molecular Function

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Biological Process
External links
PDB RCSB:6lgi, PDBe:6lgi, PDBj:6lgi
PDBsum6lgi
PubMed32381508
UniProtA0A077JI83

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