Structure of PDB 8b0p Chain A

Receptor sequence
>8b0pA (length=505) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
ASLIERQRIRLLLALLFGACGTLAFSPYDVWPAAIISLMGLQALTFNRRP
LQSAAIGFCWGFGLFGSGINWVYVSIATFGGMPGPVNIFLVVLLAAYLSL
YTGLFAGVLSRLWPKTTWLRVAIAAPALWQVTEFLRGWVLTGFPWLQFGY
SQIDGPLKGLAPIMGVEAINFLLMMVSGLLALALVKRNWRPLVVAVVLFA
LPFPLRYIQWFTPQPEKTIQVSMVQGDIPQSLKWDEGQLLNTLKIYYNAT
APLMGKSSLIIWPESAITDLEINQQPFLKALDGELRDKGSSLVTGIVDAR
LNKQNRYDTYNTIITLGKGAPYSYESADRYNKNHLVPFGEFVPLESILRP
LAPFFDLPMSSFSRGPYIQPPLSANGIELTAAIAYEIILGEQVRDNFRPD
TDYLLTISNDAWFGKSIGPWQHFQMARMRALELARPLLRSTNNGITAVIG
PQGEIQAMIPQFTREVLTTNVTPTTGLTPYARTGNWPLWVLTALFGFAAV
LMSLR
3D structure
PDB8b0p Structure snapshots reveal the mechanism of a bacterial membrane lipoprotein N -acyltransferase.
ChainA
Resolution2.86 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.1.269: apolipoprotein N-acyltransferase.
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 peptide A W237 E267 P361 S363 F365 W415 W234 E264 P358 S360 F362 W412
BS02 IG7 A W74 S78 L93 L97 Y100 L143 F146 E267 V339 G342 E343 F358 A387 W415 W71 S75 L90 L94 Y97 L140 F143 E264 V336 G339 E340 F355 A384 W412
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0016410 N-acyltransferase activity
GO:0016746 acyltransferase activity
Biological Process
GO:0042158 lipoprotein biosynthetic process
Cellular Component
GO:0005886 plasma membrane
GO:0016020 membrane
GO:0030288 outer membrane-bounded periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8b0p, PDBe:8b0p, PDBj:8b0p
PDBsum8b0p
PubMed37390210
UniProtP23930|LNT_ECOLI Apolipoprotein N-acyltransferase (Gene Name=lnt)

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