Structure of PDB 6xqg Chain A Binding Site BS03

Receptor Information
>6xqg Chain A (length=250) Species: 77133 (uncultured bacterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TAPGNEPMAIPSDYKLVWADEFNTPGAPDAKKWRYDTSRNKEGWYNNELQ
YYAAGRPENVRVENGNLVIETRKERLTSMADYGGQEYSSGKLFTQGLADW
QYGYVEVRAKLACGKGMWPAIWMMASDGSTGWPALGSIDIMEMVAWDPTT
IHGTIHTKAYNTQKGSRTTAADPCGQFHTYSLDWTKDRMLIGVDGHAYMR
FDNDHKGNHDTWPFDSPQYLILNVAIGGWGVDAAAFPSKMEVDYVRVYQK
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 chain6xqg Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6xqg Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on beta-1,3 and beta-1,4 glycosidic bonds.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		E28 G72 D258
Binding residue
(residue number reindexed from 1)		E21 G65 D243
Annotation score4
Enzymatic activity
Enzyme Commision number 3.2.1.39: glucan endo-1,3-beta-D-glucosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0042973 glucan endo-1,3-beta-D-glucosidase 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:6xqg, PDBe:6xqg, PDBj:6xqg
PDBsum6xqg
PubMed33556371
UniProtA0A0B5H9B3

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