Structure of PDB 7esc Chain A Binding Site BS02

Receptor Information
>7esc Chain A (length=322) Species: 393133 (Listeria monocytogenes 10403S) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KLMDQPYSKTDFLMGTVVTLKIYDKGKEDVLDKGFDRIKDLAAKITTSDS
EKTSEVDKINEQAGKKPVKVSEDVYYLIQEGLKYSENSGGSFDITIGPLT
SLWHIGFSDARKPSQAEIDAVLPLINYKDVKMNDKDQTVYLEKEGMELDL
GAIAKGFITDETLKVFKENKVTTSIIDLGGNIYVQGNNPNGNKWNVGIQD
PFSPRGSVIGKLPESNMSIVTSGIYERYLEVDGKTYHHILDPKTGYPFDN
DIAGVSIVSKKSIDGDGLSTATFSKGIKGGMDYIEQFEGVDAIFISKEKK
VYETSGLKGQFELTDKDFQMDT
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain7esc Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7esc Structural insights into the catalytic and inhibitory mechanisms of the flavin transferase FmnB in Listeria monocytogenes.
Resolution2.201 Å
Binding residue
(original residue number in PDB)
A187 D301
Binding residue
(residue number reindexed from 1)
A152 D266
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.1.180: FAD:protein FMN transferase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0017013 protein flavinylation
Cellular Component
GO:0005886 plasma membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7esc, PDBe:7esc, PDBj:7esc
PDBsum7esc
PubMed35281791
UniProtA0A0H3GJF7

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