Structure of PDB 3rwk Chain X

Receptor sequence
>3rwkX (length=493) Species: 5058 (Aspergillus ficuum) [Search protein sequence]
QSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQHNPTANVWGNICWG
HATSTDLMHWAHKPTAIADENGVEAFTGTAYYDPNNTSGLGDSANPPYLA
WFTGYTTSSQTQDQRLAFSVDNGATWTKFQGNPIISTSQEAPHDITGGLE
SRDPKVFFHRQSGNWIMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSIN
GLSSDITGWEVPDMFELPVEGTEETTWVVMMTPAEGSPAGGNGVLAITGS
FDGKSFTADPVDASTMWLDNGRDFDGALSWVNVPASDGRRIIAAVMNSYG
SNPPTTTWKGMLSFPRTLSLKKVGTQQHFVQQPITELDTISTSLQILANQ
TITPGQTLLSSIRGTALDVRVAFYPDAGSVLSLAVRKGASEQTVIKYTQS
DATLSVDRTESGDISYDPAAGGVHTAKLEEDGTGLVSIRVLVDTCSVEVF
GGQGEAVISDLIFPSDSSDGLALEVTGGNAVLQSVDVRSVSLE
3D structure
PDB3rwk First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity.
ChainX
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.7: inulinase.
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 MAN X P441 A442 P418 A419
BS02 MAN X R295 D440 P441 R272 D417 P418
BS03 MAN X G264 N265 R295 S321 G241 N242 R272 S298
BS04 FRU X W40 M41 N42 N61 N320 G323 W17 M18 N19 N38 N297 G300
BS05 FRU X E43 F99 T100 R175 D176 E233 E20 F76 T77 R152 D153 E210
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:3rwk, PDBe:3rwk, PDBj:3rwk
PDBsum3rwk
PubMed22750808
UniProtO94220|INU2_ASPFI Extracellular endo-inulinase inu2 (Gene Name=inu2)

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