Structure of PDB 6xqg Chain A

Receptor sequence
>6xqgA (length=250) Species: 77133 (uncultured bacterium) [Search protein sequence]
TAPGNEPMAIPSDYKLVWADEFNTPGAPDAKKWRYDTSRNKEGWYNNELQ
YYAAGRPENVRVENGNLVIETRKERLTSMADYGGQEYSSGKLFTQGLADW
QYGYVEVRAKLACGKGMWPAIWMMASDGSTGWPALGSIDIMEMVAWDPTT
IHGTIHTKAYNTQKGSRTTAADPCGQFHTYSLDWTKDRMLIGVDGHAYMR
FDNDHKGNHDTWPFDSPQYLILNVAIGGWGVDAAAFPSKMEVDYVRVYQK
3D structure
PDB6xqg Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on beta-1,3 and beta-1,4 glycosidic bonds.
ChainA
Resolution2.15 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.39: glucan endo-1,3-beta-D-glucosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLC A N53 W125 A127 W129 W139 D146 E149 H163 N46 W118 A120 W122 W132 D139 E142 H156
BS02 BGC A N53 W139 N46 W132
BS03 CA A E28 G72 D258 E21 G65 D243
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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