Structure of PDB 1z6l Chain B

Receptor sequence
>1z6lB (length=484) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGR
KYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRV
DHDKELLLEIVDNEMSKFAELEFHSDCSFFQLVMKYLLQRRQFLTNDQIR
YLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQRIAQSF
PQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSVLNLSV
QPNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNESSKIV
TLANSTNEFVEIVRNAENLDELDSMLERTSVTCWSQPLFFVNLSKSTGVA
SFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSEDVIDGMRP
ENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPVDMVVAMSNGQDSRIR
FAGEHTIMDGAGCAYGAWESGRREATRISDLLKL
3D structure
PDB1z6l crystal structure of Fms1 and its complex with spermine reveal substrate specificity
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H67
Catalytic site (residue number reindexed from 1) H60
Enzyme Commision number 1.5.3.17: non-specific polyamine oxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0003682 chromatin binding
GO:0016491 oxidoreductase activity
GO:0046592 polyamine oxidase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0052897 N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
GO:0052901 spermine oxidase activity
GO:0052903 N(1)-acetylpolyamine oxidase (3-acetamidopropanal-forming) activity
Biological Process
GO:0006338 chromatin remodeling
GO:0015940 pantothenate biosynthetic process
GO:0046208 spermine catabolic process
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:1z6l, PDBe:1z6l, PDBj:1z6l
PDBsum1z6l
PubMed
UniProtP50264|FMS1_YEAST Polyamine oxidase FMS1 (Gene Name=FMS1)

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