Structure of PDB 6xqm Chain A

Receptor sequence
>6xqmA (length=263) Species: 77133 (uncultured bacterium) [Search protein sequence]
PEGVTAPGNEPMAIPSDYKLVWADEFNTPGAPDAKKWRYDTSRNKEGWYN
NELQYYAAGRPENVRVENGNLVIETRKERLTSMADYGGQEYSSGKLFTQG
LADWQYGYVEVRAKLACGKGMWPAIWMMASDGSTGWPALGSIDIMEMVAW
DPTTIHGTIHTKAYNHVIHTQKGSRTTAADPCGQFHTYSLDWTKDRMLIG
VDGHAYMRFDNDHKGNHDTWPFDSPQYLILNVAIGGWGGQQGVDAAAFPS
KMEVDYVRVYQKR
3D structure
PDB6xqm Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on beta-1,3 and beta-1,4 glycosidic bonds.
ChainA
Resolution1.85 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 D146 E149 H169 N50 W122 A124 W126 D143 E146 H166
BS02 BGC A Y52 N53 M131 W139 H169 Y49 N50 M128 W136 H166
BS03 GLC A E149 T161 H163 H169 Q174 W240 E146 T158 H160 H166 Q171 W237
BS04 CA A E28 N30 G72 D258 E25 N27 G69 D255
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:6xqm, PDBe:6xqm, PDBj:6xqm
PDBsum6xqm
PubMed33556371
UniProtA0A0B5H9B3

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