Structure of PDB 6nxj Chain A Binding Site BS03

Receptor Information
>6nxj Chain A (length=307) Species: 666 (Vibrio cholerae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AEQVHLSGPTMGTTYNIKYIQQPGIADSKTLQTEIDRLLEEVNDQMSTYR
KDSELSRFNQHTSSEPFAVSTQTLTVVKEAIRLNGLTEGALDVTVGPLVN
LWGFGPEARPDVVPTDEELNARRAITGIEHLTIEGNTLSKDIPELYVDLS
TIAKGWGVDVVADYLQSQGIENYMVEIGGEIRLKGLNRDGVPWRIAIEKP
SVQEIIEPGDYAIATSGDYRNYFEQDGVRYSGIIDPTTGRPINNRVVSVT
VLDKSCMTADGLATGLMVMGEERGMAVAEANQIPVLMIVKTDDGFKEYAS
SSFKPFL
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 chain6nxj Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6nxj Conserved residue His-257 ofVibrio choleraeflavin transferase ApbE plays a critical role in substrate binding and catalysis.
Resolution1.92 Å
Binding residue
(original residue number in PDB)
E200 D285
Binding residue
(residue number reindexed from 1)
E180 D260
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.1.180: FAD:protein FMN transferase.
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0017013 protein flavinylation
Cellular Component
GO:0005886 plasma membrane

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6nxj, PDBe:6nxj, PDBj:6nxj
PDBsum6nxj
PubMed31350338
UniProtA5F5Y3|APBE_VIBC3 FAD:protein FMN transferase (Gene Name=apbE)

[Back to BioLiP]