Structure of PDB 4q23 Chain A

Receptor sequence

>4q23A (length=337) Species: 9606 (Homo sapiens)

VYAQEKQDFVQHFSQIVRVLTGHPEIGDAIARLKEVLEYNAIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKAAFYSFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIY

3D structure

• PDB: 4q23 The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
• Chain: A
• Resolution: 1.98 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): 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	RIS	A	L100 D103 R112 Q171 K200 D243 K257	L88 D91 R100 Q159 K188 D231 K245	BindingDB: IC50=11nM,Ki=82.2nM
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

External links

• PDB: RCSB:4q23, PDBe:4q23, PDBj:4q23
• PDBsum: 4q23
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)