Structure of PDB 3lih Chain A

Receptor sequence
>3lihA (length=634) Species: 34381 (Aspergillus japonicus) [Search protein sequence]
SYHLDTTAPPPTNLSTLPNNTLFHLWRPRAHILPAEGQIGDPCAHYTDPS
TGLFHVGFLHDGDGIAGATTANLATYTDTSDNGSFLIQPGGKNDPVAVFD
GAVIPVGVNNTPTLLYTSVSFLPIHWSIPYTRGSETQSLAVARDGGRRFD
KLDQGPVIADHPFAVDVTAFRAPFVFRSARLDVLLSLDEEVARNETAVQQ
AVDGWTEKNAPWYVAVSGGVHGVGPAQFLYRQNGGNASEFQYWEYLGEWW
QEATNSSWGDEGTWAGRWGFNFETGNVLFLTEEGHDPQTGEVFVTLGTEG
SGLPIVPQVSSIHDMLWAAGEVGVGSEQEGAKVEFSPSMAGFLDWGFSAY
AAAGKVLPASSAVSKTSGVEVDRYVSFVWLTGDQYEQADGFPTAQQGWTG
SLLLPRELKVQTVENVVDNELVREEGVSWVVGESDNQTATLRTLGITIAR
ETKAALLANGSVTAEEDRTLQTAAVVPFAQSPSSKFFVLTAQLEFPASAR
SSPLQSGFEILASELERTAIYYQFSNESLVVDRSQTSAAAPTNPGLDSFT
ESGKLRLFDVIENGQEQVETLDLTVVVDNAVVEVYANGRFALSTWARSWY
DNSTQIRFFHNGEGEVQFRNVSVSEGLYNAWPER
3D structure
PDB3lih Crystal structures of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete subsites in the active site for catalysis
ChainA
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 FRU A D60 D119 R190 E292 D41 D100 R171 E273
BS02 GLC A I143 H144 E292 E318 I124 H125 E273 E299
BS03 GLA A P142 I143 Q327 P123 I124 Q308
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:3lih, PDBe:3lih, PDBj:3lih
PDBsum3lih
PubMed20466731
UniProtQ1W3Z7

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