Structure of PDB 1zw5 Chain A

Receptor sequence
>1zw5A (length=339) Species: 9606 (Homo sapiens) [Search protein sequence]
EKQDFVQHFSQIVRVLTEDEHPEIGDAIARLKEVLEYNAIGGKYNRGLTV
VVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSS
YQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQD
NKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVF
LQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK
3D structure
PDB1zw5 The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K71 F112 D117 D121 R126 D188 K214 F253 D257 D258
Catalytic site (residue number reindexed from 1) K43 F84 D89 D93 R98 D160 K186 F225 D229 D230
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 D117 D121 D89 D93
BS02 MG A D117 D121 D89 D93
BS03 IPE A G70 K71 R74 Q110 R127 D257 G42 K43 R46 Q82 R99 D229
BS04 ZOL A D117 R126 K214 T215 D257 K271 D89 R98 K186 T187 D229 K243 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

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Molecular Function
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Biological Process
External links
PDB RCSB:1zw5, PDBe:1zw5, PDBj:1zw5
PDBsum1zw5
PubMed16684881
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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