Structure of PDB 2ogd Chain A

Receptor sequence
>2ogdA (length=358) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNR
GLTVIDVAESLLSLDGARRKRVLHDACVCGWMIEFLQAHYLVEDDIMDNS
VTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFADRPFLQDLLC
RFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEFTLSNYKRIV
KYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEYFQVQDDVMD
CFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKANYGSGDSEK
VATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPGFAASVETLW
GKTYKRQK
3D structure
PDB2ogd Bisphosphonates: Teaching Old Drugs with New Tricks
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) K47 H89 D94 D98 R103 D166 K203 F242 D246 D247
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 D94 D98
BS02 MG A D103 D107 D94 D98
BS03 SUF A D103 R112 K212 D255 K269 D94 R103 K203 D246 K260
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:2ogd, PDBe:2ogd, PDBj:2ogd
PDBsum2ogd
PubMed
UniProtQ86C09

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