Structure of PDB 4qlj Chain A

Receptor sequence
>4qljA (length=472) Species: 39947 (Oryza sativa Japonica Group) [Search protein sequence]
NWLGGLSRAAFPKRFVFGTVTSAYQVEGMAASGGRGPSIWDAFAHTPGNV
AGNQNGDVATDQYHRYKEDVNLMKSLNFDAYRFSISWSRIFPDGEGRVNQ
EGVAYYNNLINYLLQKGITPYVNLYHYDLPLALEKKYGGWLNAKMADLFT
EYADFCFKTFGNRVKHWFTFNEPRIVALLGYDAGTNPPKRCTKCAAGGNS
ATEPYIVAHNFLLSHAAAVARYRTKYQAAQQGKVGIVLDFNWYEALSNST
EDQAAAQRARDFHIGWYLDPLINGHYPQIMQDLVKDRLPKFTPEQARLVK
GSADYIGINQYTASYMKGQQLMQQTPTSYSADWQVTAVFAKNGKPIGPQA
NSNWLYIVPWGMYGCVNYIKQKYGNPTVVITGNGMDQPANLSRDQYLRDT
TRVHFYRSYLTQLKKAIDEGANVAGYFAWSLLDNFEWLSGYTSKFGIVYV
DFNTLERHPKASAYWFRDMLKH
3D structure
PDB4qlj Effects of active site cleft residues on oligosaccharide binding, hydrolysis, and glycosynthase activities of rice BGlu1 and its mutants
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R86 H130 E176 I179 N313 Y315 G386
Catalytic site (residue number reindexed from 1) R82 H126 E172 I175 N309 Y311 G382
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 BGC A E176 Y315 E172 Y311
BS02 BGC A Q29 H130 E176 Y315 W433 E440 F449 Q25 H126 E172 Y311 W429 E436 F445
BS03 ZN A D65 H68 D61 H64
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0004567 beta-mannosidase activity
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0033907 beta-D-fucosidase activity
GO:0042803 protein homodimerization activity
GO:0042973 glucan endo-1,3-beta-D-glucosidase activity
GO:0047668 amygdalin beta-glucosidase activity
GO:0047701 beta-L-arabinosidase activity
GO:0050224 prunasin beta-glucosidase activity
GO:0080079 cellobiose glucosidase activity
GO:0080083 beta-gentiobiose beta-glucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4qlj, PDBe:4qlj, PDBj:4qlj
PDBsum4qlj
PubMed25252199
UniProtQ75I93|BGL07_ORYSJ Beta-glucosidase 7 (Gene Name=BGLU7)

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