Structure of PDB 5m1d Chain B

Receptor sequence
>5m1dB (length=465) Species: 562 (Escherichia coli) [Search protein sequence]
YNDLRDFLTLLEQQGELKRITLPVDPHLEITEIADRTLRAGGPALLFENP
KGYSMPVLCNLFGTPKRVAMGMGQEDVSALREVGKLLAFLKLNMPTKRLR
GAPCQQKIVSGDDVDLNRIPIMTCWPEDAAPLITWGLTVTRGPHKERQNL
GIYRQQLIGKNKLIMRWLSHRGGALDYQEWCAAHPGERFPVSVALGADPA
TILGAVTPVPDTLSEYAFAGLLRGTKTEVVKCISNDLEVPASAEIVLEGY
IEQGETAPEGPYGDHTGYYNEVDSFPVFTVTHITQREDAIYHSTYTGRPP
DEPAVLGVALNEVFVPILQKQFPEIVDFYLPPEGCSYRLAVVTIKKQYAG
HAKRVMMGVWSFLRQFMYTKFVIVCDDDVNARDWNDVIWAITTRMDPARD
TVLVENTPIDYLDFASPVSGLGSKMGLDATNKWPGETQREWGRPIKKDPD
VVAHIDAIWDELAIF
3D structure
PDB5m1d Oxidative Maturation and Structural Characterization of Prenylated FMN Binding by UbiD, a Decarboxylase Involved in Bacterial Ubiquinone Biosynthesis.
ChainB
Resolution2.7 Å
3D
structure
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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 B N175 E241 N149 E215
BS02 4LU B T160 N175 I178 Y179 R180 R192 L194 R197 V232 T134 N149 I152 Y153 R154 R166 L168 R171 V206
Gene Ontology
Molecular Function
GO:0008694 3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity
GO:0016831 carboxy-lyase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0120233 prenyl-FMNH2 binding
Biological Process
GO:0006744 ubiquinone biosynthetic process
GO:0032150 ubiquinone biosynthetic process from chorismate
GO:0034214 protein hexamerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
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:5m1d, PDBe:5m1d, PDBj:5m1d
PDBsum5m1d
PubMed28057757
UniProtP0AAB4|UBID_ECOLI 3-octaprenyl-4-hydroxybenzoate carboxy-lyase (Gene Name=ubiD)

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