Structure of PDB 1yhl Chain A

Receptor sequence
>1yhlA (length=362) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
MASMERFLSVYDEVQAFLLDQLQSKYEIDPNRARYLRIMMDTTCLGGKYF
RGMTVVNVAEGFLAVTQHDEATKERILHDACVGGWMIEFLQAHYLVEDDI
MDGSVMRRGKPCWYRFPGVTTQCAINDGIILKSWTQIMAWHYFADRPFLK
DLLCLFQKVDYATAVGQMYDVTSMCDSNKLDPEVAQPMTTDFAEFTPAIY
KRIVKYKTTFYTYLLPLVMGLFVSEAAASVEMNLVERVAHLIGEYFQVQD
DVMDCFTPPEQLGKVGTDIEDAKCSWLAVTFLGKANAAQVAEFKANYGDK
DPAKVAVVKRLYSEANLQADFAAYEAEVVREVESLIEQLKVKSPTFAESV
AVVWEKTHKRKK
3D structure
PDB1yhl Structure and mechanism of the farnesyl diphosphate synthase from Trypanosoma cruzi: Implications for drug design.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K48 H93 D98 D102 R107 D170 K207 F246 D250 D251
Catalytic site (residue number reindexed from 1) K48 H93 D98 D102 R107 D170 K207 F246 D250 D251
Enzyme Commision number ?
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 D98 D102 D98 D102
BS02 MG A D98 D102 D98 D102
BS03 DMA A G47 K48 F50 R51 Q91 R108 F246 K362 G47 K48 F50 R51 Q91 R108 F246 K362
BS04 RIS A L95 D98 R107 Q167 K207 T208 Y211 D250 K264 L95 D98 R107 Q167 K207 T208 Y211 D250 K264 BindingDB: IC50=27nM
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:1yhl, PDBe:1yhl, PDBj:1yhl
PDBsum1yhl
PubMed16288456
UniProtQ8WS26

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