Structure of PDB 3g59 Chain A

Receptor sequence
>3g59A (length=289) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
GAMVMRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINET
FPKWSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYILPTVFIDHDDTFK
TLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVIGIR
HTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLANIWSFLLYSNEPICEL
YRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFEWEIENRYKHNEVTKAE
PIPIADEDLVKIENLHEDYYPGWYLVDDKLERAGRIKKK
3D structure
PDB3g59 Structure and mechanism of a eukaryotic FMN adenylyltransferase.
ChainA
Resolution1.87 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.7.7.2: FAD 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 ATP A S60 Y61 N62 K65 D66 C67 F107 I108 I162 G163 I164 Y216 S222 L223 S64 Y65 N66 K69 D70 C71 F92 I93 I147 G148 I149 Y201 S207 L208
BS02 POP A A270 D271 A255 D256
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0003919 FMN adenylyltransferase activity
GO:0005524 ATP binding
GO:0016779 nucleotidyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006747 FAD 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:3g59, PDBe:3g59, PDBj:3g59
PDBsum3g59
PubMed19375431
UniProtQ6FNA9

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