Structure of PDB 2ewg Chain B

Receptor sequence

>2ewgB (length=367) Species: 5691 (Trypanosoma brucei)

MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNR
GLTVIDVAESLLSLSPNNNGEEDDGARRKRVLHDACVCGWMIEFLQAHYL
VEDDIMDNSVTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFAD
RPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEF
TLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEY
FQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKA
NYGSGDSEKVATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPG
FAASVETLWGKTYKRQK

3D structure

• PDB: 2ewg Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.
• Chain: B
• Resolution: 2.48 Å

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 H98 D103 D107 R112 D175 K212 F251 D255 D256
• 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	D103 D107	D103 D107
BS02	MG	B	D103 D107	D103 D107
BS03	M0N	B	Y99 D103 D107 R112 T168 Q172 K212 T213 Q252 D255 K269	Y99 D103 D107 R112 T168 Q172 K212 T213 Q252 D255 K269

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

External links

• PDB: RCSB:2ewg, PDBe:2ewg, PDBj:2ewg
• PDBsum: 2ewg
• PubMed: 17090032
• UniProt: Q86C09