Structure of PDB 5m1e Chain A

Receptor sequence
>5m1eA (length=469) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
YNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENP
KGYSMPVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKKQVLNMPTK
RLRGAPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKER
QNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGA
DPATILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCISNDLEVPASAEIVL
EGYIEQGETAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHSTYTG
RPPDEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRLAVVTIKKQ
YAGHAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTRMDP
ARDTVLVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETQREWGRPIKK
DPDVVAHIDAIWDELAIFN
3D structure
PDB5m1e Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.
ChainA
Resolution2.62 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 4.1.1.98: 4-hydroxy-3-polyprenylbenzoate decarboxylase.
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 MN A N175 E241 N152 E218
BS02 7D9 A T160 N175 I178 Y179 R180 R192 L194 R197 V232 E241 T137 N152 I155 Y156 R157 R169 L171 R174 V209 E218
Gene Ontology
Molecular Function
GO:0008694 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
GO:0016831 carboxy-lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006744 ubiquinone biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5m1e, PDBe:5m1e, PDBj:5m1e
PDBsum5m1e
PubMed28057757
UniProtP0AAB5|UBID_ECOL6 3-octaprenyl-4-hydroxybenzoate carboxy-lyase (Gene Name=ubiD)

[Back to BioLiP]