Structure of PDB 2p1c Chain A

Receptor sequence
>2p1cA (length=357) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNR
GLTVIDVAESLLSDGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNSV
TRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLCR
FNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIVK
YKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMDC
FTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKANYGSGDSEKV
ATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLWG
KTYKRQK
3D structure
PDB2p1c Structures of a potent phenylalkyl bisphosphonate inhibitor bound to farnesyl and geranylgeranyl diphosphate synthases.
ChainA
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K47 H98 D103 D107 R112 D175 K212 F251 D255 D256
Catalytic site (residue number reindexed from 1) K47 H88 D93 D97 R102 D165 K202 F241 D245 D246
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 A D103 D107 D93 D97
BS02 MG A D255 D259 D273 D245 D249 D263
BS03 MG A D103 D107 D175 D93 D97 D165
BS04 GG3 A Y99 D103 R112 T168 A169 Q172 K212 T213 Y216 D255 K269 Y89 D93 R102 T158 A159 Q162 K202 T203 Y206 D245 K259 MOAD: Ki=21nM
PDBbind-CN: -logKd/Ki=7.68,Ki=21nM
Gene Ontology
Molecular Function
GO:0004161 dimethylallyltranstransferase activity
GO:0004337 geranyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0045337 farnesyl diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2p1c, PDBe:2p1c, PDBj:2p1c
PDBsum2p1c
PubMed18442135
UniProtQ86C09

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