Structure of PDB 8iwf Chain A

Receptor sequence
>8iwfA (length=630) Species: 5061 (Aspergillus niger) [Search protein sequence]
VPYEEYILAPSSRDLAPASVRQVNGSVTNAAALTGAGGQATFNGVSSVTY
DFGINVAGIVSVDVASASSESAFIGVTFTESSMWISNEACDATQDAGLDT
PLWFAVGQGAGVYSVGKKYTRGAFRYMTVVSNTTATVSLNSVKINYTASP
IQDLRAYTGYFHSSDELLNRIWYAGAYTLQLCSIDPTTGDALVGLTITLP
QTDKWWTNYTITNGSSTLTDGAKRDRLVWPGDMSIALESVAVSTEDLYSV
RTALESLYALQKADGQLPYAGKPFYDTVSFTYHLHSLVGAASYYQYTGDR
AWLTRYWGQYKKGVQWALSGVDSTGLANITASADWLRFGMGAHNIEANAI
LYYVLNDAISLAQSLNDNAPIRNWTATAARIKTVANELLWDDKNGLYTDN
ETTTLHPQDGNSWAVKANLTLSANQSAIISESLAARWGPYGAPAPEAGAT
VSPFIGGFELQAHYQAGQPDRALDLLRLQWGFMLDDPRMTNSTFIEGYST
DGSLVYAPYTNRPRVSHAHGWSTGPTSALTIYTAGLRVTGPAGATWLYKP
QPGNLTQVEAGFSTRLGSFASSFSRSGGRYQELSFTTPNGTTGSVELGDV
SGQLVSEGGVKVQLVGGKASGLQGGKWRLN
3D structure
PDB8iwf Crystal structure and catalytic function of alpha-L-rhamnosidase from Aspergillus niger
ChainA
Resolution2.86 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.40: alpha-L-rhamnosidase.
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 RY3 A D95 D227 D232 W236 D239 F281 Y289 L343 E503 Y516 R521 D95 D220 D225 W229 D232 F274 Y282 L336 E496 Y509 R514
Gene Ontology
Molecular Function
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0030596 alpha-L-rhamnosidase activity
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:8iwf, PDBe:8iwf, PDBj:8iwf
PDBsum8iwf
PubMed
UniProtR9W5L0

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