Structure of PDB 1xpq Chain C Binding Site BS01

Receptor Information
>1xpq Chain C (length=499) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQ
GRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERG
RVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQF
LTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVV
QRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQ
SVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECC
WSNESSKIVTLANSTNEFVEIVRNAENLDELDSMLERTSVTCWSQPLFFV
NLSKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDS
EDVIDGMRPIENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVD
MVVAMSNGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLKLE
Ligand information
Ligand IDSPM
InChIInChI=1S/C10H26N4/c11-5-3-9-13-7-1-2-8-14-10-4-6-12/h13-14H,1-12H2
InChIKeyPFNFFQXMRSDOHW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		NCCCNCCCCNCCCN
OpenEye OEToolkits 1.5.0C(CCNCCCN)CNCCCN
FormulaC10 H26 N4
NameSPERMINE
ChEMBLCHEMBL23194
DrugBankDB00127
ZINCZINC000001532734
PDB chain1xpq Chain C Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1xpq Crystal structures of Fms1 and its complex with spermine reveal substrate specificity.
Resolution2.51 Å
Binding residue
(original residue number in PDB)		W65 H67 D94 F97 L173 W174 L294 K312 Y450
Binding residue
(residue number reindexed from 1)		W60 H62 D89 F92 L168 W169 L289 K307 Y439
Annotation score5
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.
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:1xpq, PDBe:1xpq, PDBj:1xpq
PDBsum1xpq
PubMed15843025
UniProtP50264|FMS1_YEAST Polyamine oxidase FMS1 (Gene Name=FMS1)

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