Structure of PDB 6lge Chain A Binding Site BS05

Receptor Information
>6lge 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
YTKDLIELYDVVYEWREFLDEYNKNHGGDTRVVFSEGYANVSMTMLYYGN
EDGAIGAHFPFNFDFITDLSSKSNARDFVYIILRWLTYMPYGGIPNWVFG
NHDNNRMPTRFRHDMVDGLNIINMLLPGVAVTYQGEEIGMRDGYVSWEDT
VDIEACNRGDPDTYHLYSRDPARTPYHWDNSTSAGFSTSTNTWLPVAEDY
QEINLAKQKETARSHFKNYQALTKLRKQATLSHGEYDIRALSDRTFYLVR
SLPTHDTYVLLFNVSERRDTVDLGRVPHLTLPATVYVSSIHSARLAGHEI
TSSQLSLEAGEALVLKAQPI
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 chain6lge Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6lge Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.75 Å
Binding residue
(original residue number in PDB)
N144 D217 Y251 L252 E254
Binding residue
(residue number reindexed from 1)
N108 D181 Y215 L216 E218
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D140 D247 E322 H388 D389
Catalytic site (residue number reindexed from 1) D104 D211 E286 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:6lge, PDBe:6lge, PDBj:6lge
PDBsum6lge
PubMed32381508
UniProtA0A077JI83

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