Structure of PDB 4rxa Chain A

Receptor sequence
>4rxaA (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
QEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYNRG
LTVVVAFRELVPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAA
MYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQ
DNKCSWLVVQCLQRATPEQYQIKENYGQVAVKALYEELDLPAVFLQYEED
SYSHIMALIEQYAAPLPPAVFLGLARKIYK
3D structure
PDB4rxa Farnesyl diphosphate synthase inhibitors with unique ligand-binding geometries.
ChainA
Resolution2.2 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) K46 F86 D91 D95 R100 D162 K187 F226 D230 D231
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 3F2 A K57 N59 R60 L62 T63 V66 F239 D243 G343 K347 K46 N48 R49 L51 T52 V55 F226 D230 G323 K327 MOAD: ic50=1.8uM
PDBbind-CN: -logKd/Ki=5.74,IC50=1.8uM
BindingDB: IC50=1.8e+3nM
BS02 PO4 A G56 K57 Q96 R113 G45 K46 Q84 R101
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:4rxa, PDBe:4rxa, PDBj:4rxa
PDBsum4rxa
PubMed25815158
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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