Structure of PDB 6lgb Chain A Binding Site BS02

Receptor Information
>6lgb 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
IELYDVVYEWREFLDEYNKNHGGDTRVVFSEGYANVSMTMLYYGNEDGAI
GAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFGNHDNN
RMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDTVDIEA
CNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDYQEINL
AKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVRSLPTH
DTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEITSSQL
SLEAGEALVLKAQPI
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain6lgb Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6lgb 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)		N144 D217 Y251 L252 E254
Binding residue
(residue number reindexed from 1)		N103 D176 Y210 L211 E213
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 E322 H388 D389
Catalytic site (residue number reindexed from 1) D99 D206 E281 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:6lgb, PDBe:6lgb, PDBj:6lgb
PDBsum6lgb
PubMed32381508
UniProtA0A077JI83

[Back to BioLiP]