Structure of PDB 4kqs Chain A

Receptor sequence

>4kqsA (length=340) Species: 9606 (Homo sapiens)

VYAQEKQDFVQHFSQIVRVLTEPEIGDAIARLKEVLEYNAIGGKYNRGLT
VVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRR
GQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQS
SYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFASFYLPIAAA
MYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQ
DNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAV
FLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK

3D structure

• PDB: 4kqs Crystal Structure of Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg, Risedronate and Isopentenyl Pyrophosphate
• Chain: A
• Resolution: 1.97 Å

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	K44 R47 Q83 R100 F226
BS04	RIS	A	D103 R112 Q171 K200 T201 D243 K257	D90 R99 Q158 K187 T188 D230 K244	BindingDB: IC50=11nM,Ki=82.2nM

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

External links

• PDB: RCSB:4kqs, PDBe:4kqs, PDBj:4kqs
• PDBsum: 4kqs
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)