Structure of PDB 1yhm Chain B

Receptor sequence
>1yhmB (length=362) Species: 5693 (Trypanosoma cruzi) [Search protein sequence]
MASMERFLSVYDEVQAFLLDQLQSKYEIDPNRARYLRIMMDTTCLGGKYF
RGMTVVNVAEGFLAVTQHDEATKERILHDACVGGWMIEFLQAHYLVEDDI
MDGSVMRRGKPCWYRFPGVTTQCAINDGIILKSWTQIMAWHYFADRPFLK
DLLCLFQKVDYATAVGQMYDVTSMCDSNKLDPEVAQPMTTDFAEFTPAIY
KRIVKYKTTFYTYLLPLVMGLFVSEAAASVEMNLVERVAHLIGEYFQVQD
DVMDCFTPPEQLGKVGTDIEDAKCSWLAVTFLGKANAAQVAEFKANYGDK
DPAKVAVVKRLYSEANLQADFAAYEAEVVREVESLIEQLKVKSPTFAESV
AVVWEKTHKRKK
3D structure
PDB1yhm Structure and mechanism of the farnesyl diphosphate synthase from Trypanosoma cruzi: Implications for drug design.
ChainB
Resolution2.5 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 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 B D98 D102 D98 D102
BS02 MG B D98 D102 D98 D102
BS03 AHD B R107 K207 D250 K264 R107 K207 D250 K264 MOAD: ic50=147uM
BS04 IPE B G47 K48 R51 Q91 R108 F246 D250 K362 G47 K48 R51 Q91 R108 F246 D250 K362
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:1yhm, PDBe:1yhm, PDBj:1yhm
PDBsum1yhm
PubMed16288456
UniProtQ8WS26

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