Structure of PDB 6lgh Chain A Binding Site BS03

Receptor Information
>6lgh Chain A (length=565) Species: 7091 (Bombyx mori) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VIQLDWWKNCVLYQIYPRSFKDSDGDGIGDLKGIISELKHFVDAGVDAIW
MSPIFESPMVDFGYDISNFYDIHYEYGTMEDFEELLDKAHELGLKVLLDF
VPNHASNESEYFIKSEAREPGYENFFIWADPLPNPENPGVRLPPSNWVSQ
FGGSAWEWSEKRQQYYLHQFAIQQVDFDFRNPAVKQEMFNIMKFWLDKGA
DGFRLDALPYLIEADPADHEGRYPDDPLSGLTQFESHQLGYTIPLYTKDL
IELYDVVYEWREFLDEYNKNHGGDTRVVFSQGYANVSMTMLYYGNEDGAI
GAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGNHDNN
RMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTVDIEA
CNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQEINL
AKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRSLPTH
DTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEITSSQL
SLEAGEALVLKAQPI
Ligand information
Ligand IDBGC
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-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain6lgh Chain A Residue 703 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6lgh Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		D102 Y105 H145 F211 D247 Q322 H388 D389 R455
Binding residue
(residue number reindexed from 1)		D61 Y64 H104 F170 D206 Q281 H347 D348 R414
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 Q322 H388 D389
Catalytic site (residue number reindexed from 1) D99 D206 Q281 H347 D348
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:6lgh, PDBe:6lgh, PDBj:6lgh
PDBsum6lgh
PubMed32381508
UniProtA0A077JI83

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