Structure of PDB 4xgx Chain A

Receptor sequence
>4xgxA (length=290) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TEVTVLEGKTMGTFWRASIPGIDAKRSAELKEKIQTQLDADDQLLSTNKK
DSALMRFNDSQSLSPWPVSEAMADIVTTSLRIGAKTDGAMDITVGPLVNL
WGVQIPSQEQIDAMKAKTGLQHLTVINQSHQQYLQKDLPDLYVDLSTVGE
GYAADHLARLMEQEGISRYLVSVGGALNSRGMNGEGLPWRVAIAVVDING
HGISTSGSYRNSHVIDPQTGRPIEHNLVSVTVIAPTALEADAWDTGLMVL
GPEKAKEVVRREGLAVYMITKEGDSFKTWMSPQFKSFLVS
3D structure
PDB4xgx Molecular insights into the enzymatic diversity of flavin-trafficking protein (Ftp; formerly ApbE) in flavoprotein biogenesis in the bacterial periplasm.
ChainA
Resolution1.9 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 2.7.1.180: FAD:protein FMN transferase.
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 MG A T166 D280 T284 T147 D241 T245
BS02 MG A E169 Y239 E150 Y209
BS03 ADP A D103 V106 D163 T166 S238 R240 H252 V253 I254 D91 V94 D144 T147 S208 R210 H213 V214 I215
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4xgx, PDBe:4xgx, PDBj:4xgx
PDBsum4xgx
PubMed26626129
UniProtP0AB85|APBE_ECOLI FAD:protein FMN transferase (Gene Name=apbE)

[Back to BioLiP]