Structure of PDB 4rxd Chain A

Receptor sequence
>4rxdA (length=355) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
MQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNRGL
TVIDVAESLLSDGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNSVTR
RGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLCRFN
RVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIVKYK
TAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMDCFT
PPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKANYGSGDSEKVAT
VRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLWGKT
YKRQK
3D structure
PDB4rxd Farnesyl diphosphate synthase inhibitors with unique ligand-binding geometries.
ChainA
Resolution2.0 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) K45 H86 D91 D95 R100 D163 K200 F239 D243 D244
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 D103 D107 D91 D95
BS02 MG A D103 D107 D91 D95
BS03 RIS A D103 R112 Q172 K212 T213 D255 K269 D91 R100 Q160 K200 T201 D243 K257 MOAD: ic50=300nM
PDBbind-CN: -logKd/Ki=6.52,IC50=300nM
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:4rxd, PDBe:4rxd, PDBj:4rxd
PDBsum4rxd
PubMed25815158
UniProtQ86C09

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