Structure of PDB 5ogl Chain A

Receptor sequence
>5oglA (length=707) Species: 306263 (Campylobacter lari RM2100) [Search protein sequence]
ELQQNFTDNNSIKYTAILILIAFAFSVLARLYWVAWASEFYEFFFNDQLM
ITTNDGYAFAEGARDMIAGFHQPNDLSYFGSSLSTLTYWLYSILPFSFES
IILYMSTFFASLIVVPIILIAREYKLTTYGFIAALLGSIANSYYNRTMSG
YYDTDMLVLVLPMLILLTFIRLTINKDIFTLLLSPVFIMIYLWWYPSSYS
LNFAMIGLFGLYTLVFHRKEKIFYLTIALMIIALSMLAWQYKLALIVLLF
AIFAFKEEKINFYMIWALIFISILILHLSGGLDPVLYQLKFYVFKASDVQ
NLKDAAFMYFNVNETIMEVNTIDPEVFMQRISSSVLVFILSFIGFILLLK
DHKSMLLALPMLALGFMALRAGLRFTIYAVPVMALGFGYFLYAFFNFLEK
KQIKLSLRNKNILLILIAFFSISPALMHIYYYKSSTVFTSYEASILNDLK
NKAQREDYVVAWWDYGYPIRYYSDVKTLIDGGKHLGKDNFFSSFVLSKEQ
IPAANMARLSVEYTEKSFKENYPDVLKAMVKDYQKTSAKDFLESLNDPNF
KIDTPKTRDVYIYMPYRMLRIMPVVAQFANTNPDNGEQEKSLFFSQANPL
DQDGSITLDNGVEISNDYRSLKIEGNSIPLKAFVDIESITNGKFYYNEID
SKAQIYLLYLREYKSYVILDESLYNSSYIQMFLLNQYDQDLFEQITNDTR
AKIYRLK
3D structure
PDB5ogl Molecular basis of lipid-linked oligosaccharide recognition and processing by bacterial oligosaccharyltransferase.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.99.19: undecaprenyl-diphosphooligosaccharide--protein glycotransferase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004576 oligosaccharyl transferase activity
GO:0016757 glycosyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006486 protein glycosylation
GO:0018279 protein N-linked glycosylation via asparagine
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ogl, PDBe:5ogl, PDBj:5ogl
PDBsum5ogl
PubMed29058712
UniProtB9KDD4|PGLB_CAMLR Undecaprenyl-diphosphooligosaccharide--protein glycotransferase (Gene Name=pglB)

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