Structure of PDB 4ng6 Chain A

Receptor sequence

>4ng6A (length=344) Species: 9606 (Homo sapiens)

YAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGKYN
RGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSS
LTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIEL
FLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYLTAFYSFYLP
IAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIG
TDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELD
LPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK

3D structure

• PDB: 4ng6 The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
• Chain: A
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K57 F98 D103 D107 R112 D174 L200 F239 D243 D244
• Catalytic site (residue number reindexed from 1): K48 F89 D94 D98 R103 D165 L191 F230 D234 D235
• 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	D94 D98
BS02	MG	A	D103 D107	D94 D98
BS03	IPE	A	K57 R60 Q96 R113 T201 F239 D243	K48 R51 Q87 R104 T192 F230 D234
BS04	RIS	A	D103 R112 L200 T201 D243 K257	D94 R103 L191 T192 D234 K248	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:4ng6, PDBe:4ng6, PDBj:4ng6
• PDBsum: 4ng6
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)