Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VRG

Structural insights into lipoprotein N-acylation by Escherichia coli apolipoprotein N-acyltransferase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0016410molecular_functionN-acyltransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042158biological_processlipoprotein biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue OLC A 601
ChainResidue
AILE79
ATRP237
AGLY342
AGLU343
APHE365
ATRP415
APLM607

site_idAC2
Number of Residues3
Detailsbinding site for residue LNK A 602
ChainResidue
ALEU347
ALEU143
APRO346

site_idAC3
Number of Residues8
Detailsbinding site for residue PLM A 603
ChainResidue
ALEU19
AALA22
ACYS23
ATHR25
ALEU26
ATYR31
ASER70
AASN73

site_idAC4
Number of Residues7
Detailsbinding site for residue PLM A 604
ChainResidue
ALEU54
ALEU103
ALEU107
ATYR210
AGLN212
AGLN455
AHOH718

site_idAC5
Number of Residues4
Detailsbinding site for residue PLM A 605
ChainResidue
APHE92
ATRP121
AMET178
AARG193

site_idAC6
Number of Residues7
Detailsbinding site for residue PLM A 606
ChainResidue
AILE7
AGLU8
AARG13
AALA46
AASN50
ATHR119
AVAL188

site_idAC7
Number of Residues5
Detailsbinding site for residue PLM A 607
ChainResidue
ALEU97
ALEU143
APHE146
APHE416
AOLC601

site_idAC8
Number of Residues3
Detailsbinding site for residue CL A 608
ChainResidue
ALYS236
ATRP237
AASN412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues133
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues48
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28885614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28885614","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01148","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28675161","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon