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Structure of PDB 3g5a Chain E

Receptor sequence >3g5aE (length=286) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence] MRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPKW SPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIFPLTKLPTVFIDHDDTF KTLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVIGI RHTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLANIWSFLLYSNEPICE LYRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFEWEIENRYKHNEVTKA EPIPIADEDLVKIENLHEDYYPGWYLVDDKLERAGR

3D structure PDB 3g5a Structure and mechanism of a eukaryotic FMN adenylyltransferase. Chain E Resolution 1.95 Å 3D structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

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 APC E S60 N62 G64 K65 D66 C67 I108 M143 I162 G163 Y216 L223 S60 N62 G64 K65 D66 C67 I94 M129 I148 G149 Y202 L209 BS02 FMN E F147 I162 I164 D168 P169 T180 D181 W184 F187 R189 F133 I148 I150 D154 P155 T166 D167 W170 F173 R175

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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