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5AZC

Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008961molecular_functionphosphatidylglycerol-prolipoprotein diacylglyceryl transferase activity
A0009898cellular_componentcytoplasmic side of plasma membrane
A0016740molecular_functiontransferase activity
A0042158biological_processlipoprotein biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue PGT A 301
ChainResidue
ASER123
APGT310
APHE124
APHE125
AASN159
APHE160
APRO161
ATYR201
ALEU204
APHE245

site_idAC2
Number of Residues2
Detailsbinding site for residue PGT A 302
ChainResidue
AMET29
AGLY207

site_idAC3
Number of Residues2
Detailsbinding site for residue PGT A 303
ChainResidue
ATYR282
APGT308

site_idAC4
Number of Residues3
Detailsbinding site for residue PGT A 304
ChainResidue
AASN59
AGLY71
AVAL112

site_idAC5
Number of Residues2
Detailsbinding site for residue PGT A 305
ChainResidue
APHE36
AARG47

site_idAC6
Number of Residues5
Detailsbinding site for residue PGT A 307
ChainResidue
AGLU10
APHE11
AASP12
ATRP25
AMET29

site_idAC7
Number of Residues5
Detailsbinding site for residue PGT A 308
ChainResidue
ATYR217
AARG222
APHE238
ATYR282
APGT303

site_idAC8
Number of Residues16
Detailsbinding site for residue PGT A 309
ChainResidue
ATYR26
ATYR30
APHE34
APHE69
AVAL95
ATRP96
AGLY99
AMET100
AGLY138
AASN149
AGLU151
AGLY254
AALA255
ATRP256
AVAL257
AHOH426

site_idAC9
Number of Residues12
Detailsbinding site for residue PGT A 310
ChainResidue
ATYR30
APHE102
ALEU139
AGLY142
AARG143
ALEU204
ATYR235
ATYR259
APRO269
AMET270
AALA273
APGT301

Functional Information from PROSITE/UniProt
site_idPS01311
Number of Residues13
DetailsLGT Prolipoprotein diacylglyceryl transferase signature. GRlGNFINgElwG
ChainResidueDetails
AGLY142-GLY154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues135
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26729647, ECO:0000312|PDB:5AZB
ChainResidueDetails
ATRP25-ARG43
AVAL57-TYR76
AGLY99-ARG119
APHE130-GLY150
ASER198-ILE218
AALA226-PHE244
AMET262-TYR282

site_idSWS_FT_FI2
Number of Residues27
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26729647, ECO:0000305|PubMed:22287519
ChainResidueDetails
AARG44-GLU56
ATHR120-ASP129
AARG219-GLY225

site_idSWS_FT_FI3
Number of Residues83
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:26729647, ECO:0000305|PubMed:22287519
ChainResidueDetails
AVAL77-GLY98
AGLU151-PRO197
APHE245-SER261

site_idSWS_FT_FI4
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26729647, ECO:0000305|PubMed:15919996, ECO:0000305|PubMed:22287519
ChainResidueDetails
AARG283-SER291

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01147, ECO:0000269|PubMed:26729647
ChainResidueDetails
AARG143

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PDB entries from 2024-07-31

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