Structure of PDB 3cns Chain A

Receptor sequence
>3cnsA (length=492) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQ
GRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERG
RVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQF
LTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVV
QRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQ
SVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECC
WSNESSKIVTLANSTNEFVEIVRNAENLDELDSMLERTSVTCWSQPLFFV
NLSKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDS
EDVIDGMRPANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMVVAMS
NGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLKL
3D structure
PDB3cns Crystal structure of fms1 in complex with S-Bz-MeSpermidine
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H67
Catalytic site (residue number reindexed from 1) H62
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3cns, PDBe:3cns, PDBj:3cns
PDBsum3cns
PubMed
UniProtP50264|FMS1_YEAST Polyamine oxidase FMS1 (Gene Name=FMS1)

[Back to BioLiP]