Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 6lgc Chain A Binding Site BS03

Receptor Information
>6lgc 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 IDNOJ
InChIInChI=1S/C6H13NO4/c8-2-3-5(10)6(11)4(9)1-7-3/h3-11H,1-2H2/t3-,4+,5-,6-/m1/s1
InChIKeyLXBIFEVIBLOUGU-JGWLITMVSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01OC1C(NCC(O)C1O)CO
OpenEye OEToolkits 1.7.0C1C(C(C(C(N1)CO)O)O)O
OpenEye OEToolkits 1.7.0C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)O)O
CACTVS 3.370OC[CH]1NC[CH](O)[CH](O)[CH]1O
CACTVS 3.370OC[C@H]1NC[C@H](O)[C@@H](O)[C@@H]1O
FormulaC6 H13 N O4
Name1-DEOXYNOJIRIMYCIN;
MORANOLINE
ChEMBLCHEMBL307429
DrugBankDB03206
ZINCZINC000003794714
PDB chain6lgc Chain A Residue 703 [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]
PDB6lgc Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17exo-alpha-glucosidases.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		D102 Y105 H145 F211 D247 E322 H388 D389 R455
Binding residue
(residue number reindexed from 1)		D66 Y69 H109 F175 D211 E286 H352 D353 R419
Annotation score1
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

View graph for
Molecular Function
View graph for
Biological Process
External links

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417