Structure of PDB 1byh Chain A Binding Site BS03

Receptor Information
>1byh Chain A (length=214) Species: 32630 (synthetic construct) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QTGGSFFEPFNSYNSGTWEKADGYSNGGVFNCTWRANNVNFTNDGKLKLG
LTSSAYNKFDCAEYRSTNIYGYGLYEVSMKPAKNTGIVSSFFTYTGPAHG
TQWDEIDIEFLGKDTTKVQFNYYTNGVGGHEKVISLGFDASKGFHTYAFD
WQPGYIKWYVDGVLKHTATANIPSTPGKIMMNLWNGTGVDDWLGSYNGAN
PLYAEYDWVKYTSN
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 chain1byh Chain A Residue 218 [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]
PDB1byh Molecular and active-site structure of a Bacillus 1,3-1,4-beta-glucanase.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		P9 F10 G45 D207
Binding residue
(residue number reindexed from 1)		P9 F10 G45 D207
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E105 D107 E109
Catalytic site (residue number reindexed from 1) E105 D107 E109
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1byh, PDBe:1byh, PDBj:1byh
PDBsum1byh
PubMed8099449
UniProtP23904|GUB_PAEMA Beta-glucanase

[Back to BioLiP]