Structure of PDB 3o5s Chain A Binding Site BS01

Receptor Information
>3o5s Chain A (length=213) Species: 1423 (Bacillus subtilis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TGGSFFDPFNGYNSGFWQKADGYSNGNMFNCTWRANNVSMTSLGEMRLAL
TSPAYNKFDCGENRSVQTYGYGLYEVRMKPAKNTGIVSSFFTYTGPTDGT
PWDEIDIEFLGKDTTKVQFNYYTNGAGNHEKIVDLGFDAANAYHTYAFDW
QPNSIKWYVDGQLKHTATNQIPTTPGKIMMNLWNGTGVDEWLGSYNGVNP
LYAHYDWVRYTKK
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 chain3o5s Chain A Residue 243 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3o5s Biochemical and structural characterization of a Beta-1,3 1,4-glucanase from Bacillus subtilis 168
Resolution2.2 Å
Binding residue
(original residue number in PDB)		P37 G73 D235
Binding residue
(residue number reindexed from 1)		P8 G44 D206
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E133 D135 E137
Catalytic site (residue number reindexed from 1) E104 D106 E108
Enzyme Commision number 3.2.1.73: licheninase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042972 licheninase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3o5s, PDBe:3o5s, PDBj:3o5s
PDBsum3o5s
PubMed
UniProtP04957|GUB_BACSU Beta-glucanase (Gene Name=bglS)

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