Structure of PDB 3gnr Chain A

Receptor sequence
>3gnrA (length=478) Species: 39947 (Oryza sativa Japonica Group) [Search protein sequence]
GLTRGSFPEGFVFGTASAAYQYEGAVKEDGRGQTIWDTFAHTFGKITDFS
NADVAVDQYHRFEEDIQLMADMGMDAYRFSIAWSRIYPNGVGQVNQAGID
HYNKLIDALLAKGIQPYVTLYHWDLPQALEDKYKGWLDRQIVDDFAAYAE
TCFREFGDRVKHWITLNEPHTVAIQGYDAGLQAPGRCSVLLHLYCKAGNS
GTEPYVVAHHFILAHAAAASIYRTKYKATQNGQLGIAFDVMWFEPMSNTT
IDIEAAKRAQEFQLGWFADPFFFGDYPATMRARVGERLPRFTADEAAVVK
GALDFVGINHYTTYYTRHNNTNIIGTLLNNTLADTGTVSLPFKNGKPIGD
RANSIWLYIVPRGMRSLMNYVKERYNSPPVYITENGMDDSNNPFISIKDA
LKDSKRIKYHNDYLTNLAASIKEDGCDVRGYFAWSLLDNWEWAAGYSSRF
GLYFVDYKDNLKRYPKNSVQWFKALLKT
3D structure
PDB3gnr Structural and enzymatic characterization of Os3BGlu6, a rice beta-glucosidase hydrolyzing hydrophobic glycosides and (1->3)- and (1->2)-linked disaccharides.
ChainA
Resolution1.81 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R88 H132 E178 T181 N319 Y321 E394
Catalytic site (residue number reindexed from 1) R78 H122 E168 T171 N309 Y311 E384
Enzyme Commision number 3.2.1.21: beta-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 G2F A Q31 H132 N177 Y321 E394 W444 E451 W452 F460 Q21 H122 N167 Y311 E384 W434 E441 W442 F450
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3gnr, PDBe:3gnr, PDBj:3gnr
PDBsum3gnr
PubMed19587102
UniProtQ8L7J2|BGL06_ORYSJ Beta-glucosidase 6 (Gene Name=BGLU6)

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