Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8AQ2

In meso structure of the membrane integral lipoprotein N-acyltransferase Lnt from P. aeruginosa covalently linked with TITC

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0016020cellular_componentmembrane
A0016410molecular_functionN-acyltransferase activity
A0016746molecular_functionacyltransferase activity
A0042158biological_processlipoprotein biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue OLC A 601
ChainResidue
AALA20
ALEU21
AOLC605

site_idAC2
Number of Residues10
Detailsbinding site for residue OLC A 602
ChainResidue
ATRP409
APHE410
AOLC603
AQGT611
ALEU91
APHE95
AGLU269
APRO335
APHE336
AGLY337

site_idAC3
Number of Residues5
Detailsbinding site for residue OLC A 603
ChainResidue
ASER76
ALEU238
APHE336
AILE350
AOLC602

site_idAC4
Number of Residues6
Detailsbinding site for residue OLC A 604
ChainResidue
APHE95
AGLY98
AVAL99
APHE101
APHE336
ATYR339

site_idAC5
Number of Residues7
Detailsbinding site for residue OLC A 605
ChainResidue
AASP30
ATYR31
ATRP32
APRO33
ALEU34
ALEU37
AOLC601

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 606
ChainResidue
AARG47
AVAL183

site_idAC7
Number of Residues5
Detailsbinding site for residue OLC A 607
ChainResidue
ALYS52
ATRP56
APHE101
AOLC609
AHOH706

site_idAC8
Number of Residues5
Detailsbinding site for residue OLC A 608
ChainResidue
AGLY67
AVAL75
ALEU93
ATHR96
ATHR412

site_idAC9
Number of Residues6
Detailsbinding site for residue OLC A 609
ChainResidue
ATRP9
ATRP56
ATRP60
AGLY94
AGLY98
AOLC607

site_idAD1
Number of Residues3
Detailsbinding site for residue OLC A 610
ChainResidue
ALEU494
ATRP495
AGLY499

site_idAD2
Number of Residues9
Detailsbinding site for residue QGT A 611
ChainResidue
APHE95
ALEU142
ATHR143
APHE145
ALYS330
ACYS382
ATYR383
AHIS419
AOLC602

site_idAD3
Number of Residues2
Detailsbinding site for residue QGT A 612
ChainResidue
ACYS113
AHOH721

site_idAD4
Number of Residues1
Detailsbinding site for residue FLC A 613
ChainResidue
ATYR314

site_idAD5
Number of Residues2
Detailsbinding site for residue GOL A 614
ChainResidue
ATYR211
AHIS215

site_idAD6
Number of Residues2
Detailsbinding site for residue GOL A 615
ChainResidue
ATRP140
ALEU142

site_idAD7
Number of Residues1
Detailsbinding site for residue GOL A 617
ChainResidue
ATRP59

site_idAD8
Number of Residues3
Detailsbinding site for residue GOL A 618
ChainResidue
ATRP108
AARG112
AGLU292

site_idAD9
Number of Residues1
Detailsbinding site for residue GOL A 619
ChainResidue
ATRP3

site_idAE1
Number of Residues8
Detailsbinding site for residue GOL A 620
ChainResidue
AARG-3
AGLY-2
ASER-1
AHIS0
AMET1
AARG2
ATRP3
AHOH719

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues142
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_01148
ChainResidueDetails
APRO7-PHE29
AGLY58-HIS78
ALEU90-TRP110
ALEU125-PHE145
AVAL163-VAL183
AGLY192-LEU212
AVAL482-LEU502

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01148
ChainResidueDetails
AGLU269

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01148
ChainResidueDetails
ALYS330

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_01148
ChainResidueDetails
ACYS382

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon