Structure of PDB 4gdp Chain C

Receptor sequence
>4gdpC (length=488) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
KKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGR
KYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRV
DHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLT
NDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRAAFALNYDSVVQR
IAQSFPQNWLKLSCEVKSITRENVTVNCEDGTVYNADYVIITVPQSVLNL
SVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNES
SKIVTLANSTNEFVEIVRNAENLDELDSMLEREDSTSVTCWSQPLFFVNL
SKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSED
VIDGMRNKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMVVAMSNGQD
SRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLKL
3D structure
PDB4gdp Mechanistic and Structural Analyses of the Roles of Active Site Residues in Yeast Polyamine Oxidase Fms1: Characterization of the N195A and D94N Enzymes.
ChainC
Resolution1.9998 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:4gdp, PDBe:4gdp, PDBj:4gdp
PDBsum4gdp
PubMed23034052
UniProtP50264|FMS1_YEAST Polyamine oxidase FMS1 (Gene Name=FMS1)

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