Structure of PDB 4p0x Chain A

Receptor sequence
>4p0xA (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
AQEKQDFVQHFSQIVRVLTEGHPEIGDAIARLKEVLEYNAIGGKYNRGLT
VVVAFRELVEKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQ
ICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSY
QTEIGQTLDLLTAPQDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMYMAG
IDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCS
WLVVQCLQRAPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEE
DSYSHIMALIEQYAAPLPPAVFLGLARKIY
3D structure
PDB4p0x Taxodione and arenarone inhibit farnesyl diphosphate synthase by binding to the isopentenyl diphosphate site.
ChainA
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) K57 F98 D103 D107 R112 D174 K200 F239 D243 D244
Catalytic site (residue number reindexed from 1) K44 F83 D88 D92 R97 D159 K182 F221 D225 D226
Enzyme Commision number 2.5.1.1: dimethylallyltranstransferase.
2.5.1.10: (2E,6E)-farnesyl diphosphate synthase.
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 1WO A G56 K57 Y58 N59 R60 R113 F239 G43 K44 Y45 N46 R47 R98 F221 PDBbind-CN: -logKd/Ki=5.92,IC50=1.2uM
BS02 1WO A N59 K347 N46 K328 PDBbind-CN: -logKd/Ki=5.92,IC50=1.2uM
Gene Ontology
Molecular Function
GO:0004659 prenyltransferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008299 isoprenoid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4p0x, PDBe:4p0x, PDBj:4p0x
PDBsum4p0x
PubMed24927548
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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