Structure of PDB 4kqu Chain A

Receptor sequence
>4kquA (length=340) Species: 9606 (Homo sapiens) [Search protein sequence]
YAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNAIGGKYNRGLT
VVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRR
GQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQS
SYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFASFYLPIAAA
MYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQ
DNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAV
FLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
3D structure
PDB4kqu Crystal Structure of Farnesyl Synthase Mutant (Y204A) Complexed with Mg, Alendronate and Isopentenyl Pyrophosphate
ChainA
Resolution2.07 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 F85 D90 D94 R99 D161 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 MG A D103 D107 D90 D94
BS02 MG A D103 D107 D90 D94
BS03 IPE A K57 R60 Q96 R113 F239 D243 K44 R47 Q83 R100 F226 D230
BS04 AHD A D103 R112 K200 Q240 D243 K257 D90 R99 K187 Q227 D230 K244
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:4kqu, PDBe:4kqu, PDBj:4kqu
PDBsum4kqu
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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