Structure of PDB 4llt Chain A

Receptor sequence
>4lltA (length=300) Species: 375451 (Roseobacter denitrificans OCh 114) [Search protein sequence]
DLGTENLYFQSMFTQRLDAAAAAVQAHFDKVLAAFEPLPIVEAMAHATSG
GKRLRGFLVLETARLHDIAAGEAIWSATAIEALHAYSLVHDDLPCMDNDD
MRRGQPTVHKKWDDATAVLAGDALQTLAFELVTHPGASASAEVRADLALS
LARASGAQGMVLGQALDIAAETARAPLSLDEITRLQQGKTGALIGWSAQA
GARLAQADTAALKRYAQALGLAFQIADDILDVTGDSAQVGKAVGKDASAG
KATFVSLLGLDAARARAMSLIDEACDSLATYGAKADTLRETARFVVRRTH
3D structure
PDB4llt Crystal structure of a farnesyl diphosphate synthase from Roseobacter denitrificans OCh 114, target EFI-509393, with two IPP and calcium bound in active site
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D18
Catalytic site (residue number reindexed from 1) D29
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 IPE A G40 K41 R44 H73 R92 F212 D216 G51 K52 R55 H84 R103 F223 D227
BS02 IPE A S76 D80 R91 K178 K230 S87 D91 R102 K189 K241
BS03 CA A D80 D86 D91 D97
BS04 CA A D86 D156 E160 D97 D167 E171
Gene Ontology
Molecular Function
GO:0004337 geranyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid 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:4llt, PDBe:4llt, PDBj:4llt
PDBsum4llt
PubMed
UniProtQ16CN9

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