Structure of PDB 5yfb Chain B

Receptor sequence
>5yfbB (length=690) [Search protein sequence]
HRERFLADKSAPLCGMDIRKSFDQLSSKEKLYTHYVTEASWAGARIIQAQ
WTPQATDLYDLLILTFSVNGKLADLNALKTSSGLSEDDWEALIQYTVQVL
SNLVNYKTFGFTKIIPRVDAEKFESVVKASSNADQGSALFTKLKQHIYAL
SPESALFIGKRKDGHVSNYYLGEPVGDAEVDAIQNVAEKLGVDILNTRVK
KNGAGDYTLLVASAKTSPPSVHDFQIDSTPAKLTIEYGDYASSLTKVVAA
LQEAKQYTANDHQSAMIEGYVKSFNSGSIPEHKAASTEWVKDIGPVVESY
IGFVETYVDPYGGRAEWEGFTAIVDKQLSAKYEALVNGAPKLIKSLPWGT
DFEVDVFRKPDFTALEVVSFATGGIPAGINIPNYYEVRESTGFKNVSLAN
ILAAKVPNEELTFIHPDDVELYNAWDSRAFELQVANHELLGHGSGKLFQE
GADGKLNFDPEKVINPLTGKPITSWYKPGQTPDSVLGEVSSSMEECRAET
VALYLVSNLDILKIFNYVDKQDIEDIQYITFLLMARAGLRALEFYDPATK
KHGQAHMQARMGITQYLIQAGIARLELIQDANGELENLYVRVDREKVLSK
GKEVVGQLLIELQVRKSTADGTGSRDFYTTLTEPISGWEGKIRDIVLKKK
LPRKIFVQPNTFVVNGEVQLKEYPLTAAGVIESFIERRLL
3D structure
PDB5yfb Crystal structures of Aflatoxin-oxidase from Armillariella tabescens reveal a dual activity enzyme.
ChainB
Resolution2.2 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.14.4: dipeptidyl-peptidase III.
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 ZN B H443 H448 E501 H437 H442 E495
Gene Ontology
Molecular Function
GO:0004177 aminopeptidase activity
GO:0008235 metalloexopeptidase activity
GO:0008237 metallopeptidase activity
GO:0008239 dipeptidyl-peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5yfb, PDBe:5yfb, PDBj:5yfb
PDBsum5yfb
PubMed29050944
UniProtB0S4Q0

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