Structure of PDB 3g6k Chain E Binding Site BS01
Receptor Information
>3g6k Chain E (length=288) Species:
5478
(Nakaseomyces glabratus) [
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VMRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPK
WSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIVFPLTKLPTVFIDHDD
TFKTLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVI
GIRHTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLANIWSFLLYSNEPI
CELYRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFEWEIENRYKHNEVT
KAEPIPIADEDLVKIENLHEDYYPGWYLVDDKLERAGR
Ligand information
Ligand ID
POP
InChI
InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
InChIKey
XPPKVPWEQAFLFU-UHFFFAOYSA-L
SMILES
Software
SMILES
OpenEye OEToolkits 1.5.0
O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
CACTVS 3.341
O[P]([O-])(=O)O[P](O)([O-])=O
ACDLabs 10.04
[O-]P(=O)(O)OP([O-])(=O)O
OpenEye OEToolkits 1.5.0
OP(=O)([O-])OP(=O)(O)[O-]
Formula
H2 O7 P2
Name
PYROPHOSPHATE 2-
ChEMBL
DrugBank
ZINC
PDB chain
3g6k Chain E Residue 305 [
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Receptor-Ligand Complex Structure
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PDB
3g6k
Structure and mechanism of a eukaryotic FMN adenylyltransferase.
Resolution
1.35 Å
Binding residue
(original residue number in PDB)
N62 G64 K65 D66 C67 Y216 L223
Binding residue
(residue number reindexed from 1)
N63 G65 K66 D67 C68 Y204 L211
Annotation score
5
Enzymatic activity
Enzyme Commision number
2.7.7.2
: FAD synthase.
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:3g6k
,
PDBe:3g6k
,
PDBj:3g6k
PDBsum
3g6k
PubMed
19375431
UniProt
Q6FNA9
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