Structure of PDB 3g6k Chain D

Receptor sequence
>3g6kD (length=301) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
VMRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPK
WSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIVKLSQSQFDGKFHRFP
LTKLPTVFIDHDDTFKTLENFIEETSLRYSLSLYESDRDKCETMAEAFET
FLQVFPETKAIVIGIRHTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLA
NIWSFLLYSNEPICELYRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFE
WEIENRYKHNEVTKAEPIPIADEDLVKIENLHEDYYPGWYLVDDKLERAG
R
3D structure
PDB3g6k Structure and mechanism of a eukaryotic FMN adenylyltransferase.
ChainD
Resolution1.35 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 POP D N62 G64 K65 D66 C67 Y216 L223 N63 G65 K66 D67 C68 Y217 L224
BS02 FAD D S60 N62 I108 M143 F147 I160 I162 G163 T180 D181 W184 F187 R189 R297 R300 S61 N63 I109 M144 F148 I161 I163 G164 T181 D182 W185 F188 R190 R298 R301
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3g6k, PDBe:3g6k, PDBj:3g6k
PDBsum3g6k
PubMed19375431
UniProtQ6FNA9

[Back to BioLiP]