Structure of PDB 5ja0 Chain F

Receptor sequence
>5ja0F (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
YAQEKQDFVQHFSQIVRVLTEPEIGDAIARLKEVLEYNAIGGKYNRGLTV
VVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSS
YQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPIGTDIQDNKCSW
LVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEE
DSYSHIMALIEQYAAPLPPAVFLGLARKIY
3D structure
PDB5ja0 Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product.
ChainF
Resolution1.9 Å
3D
structure
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Enzymatic activity
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 PO4 F G56 K57 Q96 R113 Y349 G42 K43 Q82 R99 Y330
BS02 FPP F Y10 K57 N59 R60 V66 F239 V340 L344 K347 Y1 K43 N45 R46 V52 F225 V321 L325 K328 MOAD: Kd=5.3uM
PDBbind-CN: -logKd/Ki=5.22,Kd=6uM
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:5ja0, PDBe:5ja0, PDBj:5ja0
PDBsum5ja0
PubMed28098152
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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