Structure of PDB 4xgx Chain B Binding Site BS01

Receptor Information
>4xgx Chain B (length=293) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTNKK
DSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNL
WGFPVQIPSQEQIDAMKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTV
GEGYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIQKAVV
DINGHGISTSGSYRNHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGL
MVLGPEKAKEVVRREGLAVYMITKEGDSFKTWMSPQFKSFLVS
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 chain4xgx Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4xgx Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.
Resolution1.9 Å
Binding residue
(original residue number in PDB)
T166 D280 T284
Binding residue
(residue number reindexed from 1)
T149 D244 T248
Annotation score1
Enzymatic activity
Enzyme Commision number 2.7.1.180: FAD:protein FMN transferase.
Gene Ontology
Molecular Function
GO:0016651 oxidoreductase activity, acting on NAD(P)H
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0017013 protein flavinylation
Cellular Component
GO:0005886 plasma membrane
GO:1990204 oxidoreductase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4xgx, PDBe:4xgx, PDBj:4xgx
PDBsum4xgx
PubMed26626129
UniProtP0AB85|APBE_ECOLI FAD:protein FMN transferase (Gene Name=apbE)

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