Structure of PDB 4ni3 Chain A

Receptor sequence
>4ni3A (length=581) Species: 5518 (Fusarium graminearum) [Search protein sequence]
GPYEATWESTDKHNAAPEWYRDAKFGVYWHWGAFTTAQYASEWYPRNMYE
PDSDQRKHHTETYGPPEEWGYENFIKGAKDKKGNFVQFKPVLKSKGGEFD
PEAIIKIVKGSGARFAGPVAEHHDGFSMWDSKVNEWNPVNYGPKLDLVKL
WADLVRENDMKLVIAMHQAYNYNGFFQWAPKTNDTSLQKLLGQLPRDEED
QLWFDKHREMLDHVQPDIIWNDFSLDSPGECGSFEGPCAVDEQKRLEFLA
YYFNRGEEWGKEVVTTYKHHDHGFRNTSAVDDWERGGPSNLVRPYWQTDD
AISASSWSYTVGIKYYSSKAMVHSLLDRVSKNGNMLLNISPMANGVLPEE
QIKVLNDIGDFLSRYGEAVYDTRAWDIYGEGPNQVEGGSFTAPLQGNSSD
IRFTRNKEDDVLYVTVLGWPEDNLVSVKNLGSNALVDLESLKSVELLGDK
AGDYVKVSEWEQSKDALDITLPSQPAESLAYVLKLTFDGGIPVPQPERGA
AVFSKADATGKGVALALGTFDTVFLTEAGLKPEEIRSIRVSDGTKATLFS
GFRFTGESKELSAGEHEVEDGSVGSIVVSKI
3D structure
PDB4ni3 Structure and Substrate Specificity of a Eukaryotic Fucosidase from Fusarium graminearum.
ChainA
Resolution1.3993 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.51: alpha-L-fucosidase.
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 A D230 P232 D226 P228
Gene Ontology
Molecular Function
GO:0004560 alpha-L-fucosidase activity
GO:0015928 fucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006004 fucose metabolic process
GO:0016139 glycoside catabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4ni3, PDBe:4ni3, PDBj:4ni3
PDBsum4ni3
PubMed25086049
UniProtJ9UN47

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