Structure of PDB 1xpq Chain B

Receptor sequence

>1xpqB (length=496) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]

KKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGR
KYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRV
DHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLT
NDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQR
IAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSV
LNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWS
NESSKIVTLANSTNEFVEIVRNAENLDELDSMLERTSVTCWSQPLFFVNL
SKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSED
VIDGMRPIENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMV
VAMSNGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLKL

3D structure

PDB

1xpq Crystal structures of Fms1 and its complex with spermine reveal substrate specificity.

Chain

Resolution

2.51 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)	H60
Enzyme Commision number	1.5.3.17: non-specific polyamine oxidase.

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	SPM	B	W65 H67 W174 K312 F359 Y450 C488	W58 H60 W167 K305 F346 Y437 C475
BS02	FAD	B	G15 G17 A19 E39 A40 R41 G46 R47 G62 A63 S64 W65 H67 V223 T252 V253 G270 L294 Y445 A449 Y450 G478 E479 G487 C488 A489 A492	G8 G10 A12 E32 A33 R34 G39 R40 G55 A56 S57 W58 H60 V216 T245 V246 G263 L287 Y432 A436 Y437 G465 E466 G474 C475 A476 A479

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:1xpq, PDBe:1xpq, PDBj:1xpq
PDBsum	1xpq
PubMed	15843025
UniProt	P50264\|FMS1_YEAST Polyamine oxidase FMS1 (Gene Name=FMS1)

[Back to BioLiP]