Structure of PDB 4kq5 Chain A

Receptor sequence

>4kq5A (length=342) Species: 9606 (Homo sapiens)

VYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKY
NRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDS
SLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIE
LFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFASFYL
PIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKI
GTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEEL
DLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 4kq5 Crystal Structure of Human Farnesyl Pyrophosphate Synthase Mutant (Y204A) Complexed with Mg and Zoledronate
• Chain: A
• Resolution: 2.4 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): K49 F90 D95 D99 R104 D166 K192 F231 D235 D236
• 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	D95 D99
BS02	MG	A	D103 D107	D95 D99
BS03	ZOL	A	D103 R112 Q171 K200 T201 D243 K257	D95 R104 Q163 K192 T193 D235 K249	BindingDB: IC50=100nM,Ki=85.9nM

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:4kq5, PDBe:4kq5, PDBj:4kq5
• PDBsum: 4kq5
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)