Structure of PDB 1e55 Chain B Binding Site BS01

Receptor Information
>1e55 Chain B (length=490) Species: 4577 (Zea mays) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MLSPSEIPQRDWFPSDFTFGAATSAYQIEGAWNEDGKGESNWDHFCHNHP
ERILDGSNSDIGANSYHMYKTDVRLLKEMGMDAYRFSISWPRILPKGTKE
GGINPDGIKYYRNLINLLLENGIEPYVTIFHWDVPQALEEKYGGFLDKSH
KSIVEDYTYFAKVCFDNFGDKVKNWLTFNDPQTFTSFSYGTGVFAPGRCS
PGLDCAYPTGNSLVEPYTAGHNILLAHAEAVDLYNKHYKRDDTRIGLAFD
VMGRVPYGTSFLDKQAEERSWDINLGWFLEPVVRGDYPFSMRSLARERLP
FFKDEQKEKLAGSYNMLGLNYYTSRFSKNIDISPNYSPVLNTDDAYASQE
VNGPDGKPIGPPMGNPWIYMYPEGLKDLLMIMKNKYGNPPIYITENGIGD
VDTKETPLPMEAALNDYKRLDYIQRHIATLKESIDLGSNVQGYFAWSLLD
NFEWFAGFTERYGIVYVDRNNNCTRYMKESAKWLKEFNTA
Ligand information
Ligand IDBGC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6-/m1/s1
InChIKeyWQZGKKKJIJFFOK-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain1e55 Chain B Residue 513 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1e55 The mechanism of substrate (aglycone) specificity in beta-glucosidases is revealed by crystal structures of mutant maize beta-glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Y333 W378 E406 W457 E464 Y473
Binding residue
(residue number reindexed from 1)		Y322 W367 E395 W446 E453 Y462
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R96 H142 D191 T194 N331 Y333 E406
Catalytic site (residue number reindexed from 1) R85 H131 D180 T183 N320 Y322 E395
Enzyme Commision number 3.2.1.182: 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase.
3.2.1.21: beta-glucosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0015923 mannosidase activity
GO:0015925 galactosidase activity
GO:0015928 fucosidase activity
GO:0016162 cellulose 1,4-beta-cellobiosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0097599 xylanase activity
GO:0102726 DIMBOA glucoside beta-D-glucosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0009736 cytokinin-activated signaling pathway
Cellular Component
GO:0009507 chloroplast

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1e55, PDBe:1e55, PDBj:1e55
PDBsum1e55
PubMed11106394
UniProtP49235|HGGL1_MAIZE 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic (Gene Name=GLU1)

[Back to BioLiP]