Structure of PDB 3lfi Chain B Binding Site BS01

Receptor Information
>3lfi Chain B (length=634) Species: 34381 (Aspergillus japonicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SYHLDTTAPPPTNLSTLPNNTLFHLWRPRAHILPAEGQIGDPCAHYTDPS
TGLFHVGFLHDGDGIAGATTANLATYTDTSDNGSFLIQPGGKNDPVAVFD
GAVIPVGVNNTPTLLYTSVSFLPIHWSIPYTRGSETQSLAVARDGGRRFD
KLDQGPVIADHPFAVDVTAFRDPFVFRSARLDVLLSLDEEVARNETAVQQ
AVDGWTEKNAPWYVAVSGGVHGVGPAQFLYRQNGGNASEFQYWEYLGEWW
QEATNSSWGDEGTWAGRWGFNFETGNVLFLTEEGHDPQTGEVFVTLGTEG
SGLPIVPQVSSIHDMLWAAGEVGVGSEQEGAKVEFSPSMAGFLDWGFSAY
AAAGKVLPASSAVSKTSGVEVDRYVSFVWLTGDQYEQADGFPTAQQGWTG
SLLLPRELKVQTVENVVDNELVREEGVSWVVGESDNQTATLRTLGITIAR
ETKAALLANGSVTAEEDRTLQTAAVVPFAQSPSSKFFVLTAQLEFPASAR
SSPLQSGFEILASELERTAIYYQFSNESLVVDRSQTSAAAPTNPGLDSFT
ESGKLRLFDVIENGQEQVETLDLTVVVDNAVVEVYANGRFALSTWARSWY
DNSTQIRFFHNGEGEVQFRNVSVSEGLYNAWPER
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 chain3lfi Chain B Residue 2 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3lfi Crystal structure of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete sbusites in the active site for catalysis
Resolution2.0 Å
Binding residue
(original residue number in PDB)		I143 H144 R190 E292 E318
Binding residue
(residue number reindexed from 1)		I124 H125 R171 E273 E299
Annotation score4
Enzymatic activity
Enzyme Commision number ?
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:3lfi, PDBe:3lfi, PDBj:3lfi
PDBsum3lfi
PubMed
UniProtQ1W3Z7

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