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7ACI

In meso structure of apolipoprotein N-acyltransferase, Lnt, from Escherichia coli in 9.8 monoacylglycerol

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 PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue GOL A 601
ChainResidue
ASER363

site_idAC2
Number of Residues4
Detailsbinding site for residue GOL A 602
ChainResidue
AALA46
APRO86
AVAL89
ALH9609

site_idAC3
Number of Residues3
Detailsbinding site for residue GOL A 603
ChainResidue
ATRP141
AVAL142
ALEU143

site_idAC4
Number of Residues1
Detailsbinding site for residue GOL A 604
ChainResidue
AVAL95

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 605
ChainResidue
ALYS321
ASER506
ALEU507
AARG508

site_idAC6
Number of Residues1
Detailsbinding site for residue GOL A 606
ChainResidue
AALA203

site_idAC7
Number of Residues10
Detailsbinding site for residue LH9 A 607
ChainResidue
ASER78
AILE79
ALEU96
ATYR100
AGLY342
AGLU343
ATRP415
APHE416
ALH9608
ALH9611

site_idAC8
Number of Residues9
Detailsbinding site for residue LH9 A 608
ChainResidue
AGLU8
ALEU97
ATYR100
APHE146
APRO340
APHE341
ACYS387
ATYR388
ALH9607

site_idAC9
Number of Residues10
Detailsbinding site for residue LH9 A 609
ChainResidue
ALEU16
ALEU19
AALA22
ACYS23
ATHR25
ATYR31
ASER70
AASN73
AVAL89
AGOL602

site_idAD1
Number of Residues5
Detailsbinding site for residue LH9 A 610
ChainResidue
APHE61
ALEU103
ATYR104
AGLY106
ALEU107

site_idAD2
Number of Residues6
Detailsbinding site for residue LH9 A 611
ChainResidue
ALEU19
AGLY69
AASN73
ATYR76
AILE91
ALH9607

site_idAD3
Number of Residues4
Detailsbinding site for residue LH9 A 612
ChainResidue
ATRP121
AALA125
AMET178
AVAL197

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

221716

PDB entries from 2024-06-26

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