Structure of PDB 4kpj Chain A

Receptor sequence
>4kpjA (length=338) Species: 9606 (Homo sapiens) [Search protein sequence]
VYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNAIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFASFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
3D structure
PDB4kpj Crystal Structure of Farnesyl Pyrophosphate Synthase (Y204A) Mutant complexed with Mg, Pamidronate
ChainA
Resolution1.95 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) K45 F86 D91 D95 R100 D162 K188 F227 D231 D232
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 210 A D103 R112 K200 D243 K257 D91 R100 K188 D231 K245 BindingDB: IC50=200nM,Ki=55.9nM
BS02 MG A D103 D107 D91 D95
BS03 MG A D103 D107 D91 D95
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:4kpj, PDBe:4kpj, PDBj:4kpj
PDBsum4kpj
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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