Structure of PDB 3ldr Chain A

Receptor sequence
>3ldrA (length=634) Species: 34381 (Aspergillus japonicus) [Search protein sequence]
SYHLDTTAPPPTNLSTLPNNTLFHLWRPRAHILPAEGQIGDPCAHYTDPS
TGLFHVGFLHDGDGIAGATTANLATYTDTSDNGSFLIQPGGKNDPVAVFD
GAVIPVGVNNTPTLLYTSVSFLPIHWSIPYTRGSETQSLAVARDGGRRFD
KLDQGPVIADHPFAVDVTAFRAPFVFRSARLDVLLSLDEEVARNETAVQQ
AVDGWTEKNAPWYVAVSGGVHGVGPAQFLYRQNGGNASEFQYWEYLGEWW
QEATNSSWGDEGTWAGRWGFNFETGNVLFLTEEGHDPQTGEVFVTLGTEG
SGLPIVPQVSSIHDMLWAAGEVGVGSEQEGAKVEFSPSMAGFLDWGFSAY
AAAGKVLPASSAVSKTSGVEVDRYVSFVWLTGDQYEQADGFPTAQQGWTG
SLLLPRELKVQTVENVVDNELVREEGVSWVVGESDNQTATLRTLGITIAR
ETKAALLANGSVTAEEDRTLQTAAVVPFAQSPSSKFFVLTAQLEFPASAR
SSPLQSGFEILASELERTAIYYQFSNESLVVDRSQTSAAAPTNPGLDSFT
ESGKLRLFDVIENGQEQVETLDLTVVVDNAVVEVYANGRFALSTWARSWY
DNSTQIRFFHNGEGEVQFRNVSVSEGLYNAWPER
3D structure
PDB3ldr Crystal structure of Aspergillus japonicus fructosyltransferase complex with donor/acceptor substrates reveal complete sbusites in the active site for catalysis
ChainA
Resolution2.1 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 GLC A Y404 E405 Y385 E386
BS02 FRU A I143 R190 E292 E318 I124 R171 E273 E299
BS03 FRU A D60 L78 F118 D119 R190 E292 D41 L59 F99 D100 R171 E273
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:3ldr, PDBe:3ldr, PDBj:3ldr
PDBsum3ldr
PubMed
UniProtQ1W3Z7

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