Structure of PDB 4llt Chain B

Receptor sequence
>4lltB (length=290) Species: 375451 (Roseobacter denitrificans OCh 114) [Search protein sequence]
SMFTQRLDAAAAAVQAHFDKVLAAFEPLPIVEAMAHATSGGKRLRGFLVL
ETARLHDIAAGEAIWSATAIEALHAYSLVHDDLPCMDNDDMRRGQPTVHK
KWDDATAVLAGDALQTLAFELVTHPGASASAEVRADLALSLARASGAQGM
VLGQALDIAAETARAPLSLDEITRLQQGKTGALIGWSAQAGARLAQADTA
ALKRYAQALGLAFQIADDILDVTGDSAQVGKAVGKDASAGKATFVSLLGL
DAARARAMSLIDEACDSLATYGAKADTLRETARFVVRRTH
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
ChainB
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) D19
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 B G40 K41 R44 H73 R92 F212 D216 G41 K42 R45 H74 R93 F213 D217
BS02 IPE B D80 R91 K178 K230 D81 R92 K179 K231
BS03 CA B D80 D86 D81 D87
BS04 CA B D86 D156 D87 D157
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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