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8B0K

Cryo-EM structure of apolipoprotein N-acyltransferase Lnt from E. coli (Apo form)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006807biological_processobsolete nitrogen compound metabolic process
A0016020cellular_componentmembrane
A0016410molecular_functionN-acyltransferase activity
A0016746molecular_functionacyltransferase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042158biological_processlipoprotein biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
ChainResidueDetails
AMET1-ARG9
APHE49-ARG52
APRO117-THR120
AARG190-ASN191
AGLN509-LYS512

site_idSWS_FT_FI2
Number of Residues153
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:28675161
ChainResidueDetails
AGLN10-ALA27
ATRP34-THR48
APRO53-PHE68
AGLY87-TRP116
ATRP121-TRP141
AVAL169-LYS189
ATRP192-TYR210
AASN488-ARG508

site_idSWS_FT_FI3
Number of Residues324
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:28675161, ECO:0000269|PubMed:28885614
ChainResidueDetails
APHE28-VAL33
AGLY69-PRO86
AVAL142-GLY168
AILE211-GLY487

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
ChainResidueDetails
AGLU267

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
ChainResidueDetails
ALYS335

site_idSWS_FT_FI6
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01148, ECO:0000305|PubMed:28675161
ChainResidueDetails
ACYS387

222036

PDB entries from 2024-07-03

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