Structure of PDB 4h5c Chain F

Receptor sequence
>4h5cF (length=346) Species: 9606 (Homo sapiens) [Search protein sequence]
DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
3D structure
PDB4h5c Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme's active site closure.
ChainF
Resolution2.02 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 YS4 F F99 D103 R112 T167 E168 Q171 K200 D243 K257 F92 D96 R105 T160 E161 Q164 K193 D236 K250 PDBbind-CN: -logKd/Ki=7.55,IC50=28nM
BindingDB: IC50=28nM
BS02 PO4 F G56 K57 R60 R113 G49 K50 R53 R106
BS03 MG F D103 D107 D96 D100
BS04 MG F D103 D107 D96 D100
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4h5c, PDBe:4h5c, PDBj:4h5c
PDBsum4h5c
PubMed23234314
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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