Structure of PDB 5z3c Chain A Binding Site BS04

Receptor Information
>5z3c Chain A (length=371) Species: 479435 (Kribbella flavida DSM 17836) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GLDSHELARLHELARHSHAVITRHQDAGGAYPAAPTFSAYRGYAWLRDGS
FTAEGISRYGDVASAGRFHDWVDGVLRRRRGQVDDLLAAVDRGEVPSNEG
MLPTRFTFDGNDGSDPWWDFQTDGYGMWLWSVVTHAARHGLDLERWRAGI
DVAVDYLLAFWDRPCYDWWAEHVEHRHVSTLGAIHGGLVAVGTCAALRSA
PWSAATLQVAARIRSLVSAEGVVDGHLVKWLGSSAVDGSLPACVVPFGLV
PPDDDVAAMTRAAVAKDLDVDGGVHRFAADVFYGGGQWILLSALLGWNLA
AAGDTAGALRHLRWIADQADADGDLPEQVPHHLLHPGSRAEWVARWGTVA
TPLLWSHGMYLILADELGLLP
Ligand information
Ligand IDGOL
InChIInChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
InChIKeyPEDCQBHIVMGVHV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(CO)O)O
ACDLabs 12.01
CACTVS 3.370		OCC(O)CO
FormulaC3 H8 O3
NameGLYCEROL;
GLYCERIN;
PROPANE-1,2,3-TRIOL
ChEMBLCHEMBL692
DrugBankDB09462
ZINCZINC000000895048
PDB chain5z3c Chain A Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5z3c Structural insights reveal the second base catalyst of isomaltose glucohydrolase.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		W177 E179 R284 F290 W350
Binding residue
(residue number reindexed from 1)		W169 E171 R276 F282 W342
Annotation score1
Enzymatic activity
Enzyme Commision number 3.2.1.205: isomaltose glucohydrolase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5z3c, PDBe:5z3c, PDBj:5z3c
PDBsum5z3c
PubMed34665923
UniProtD2PPM8|IMGH_KRIFD Isomaltose glucohydrolase (Gene Name=Kfla_1896)

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