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5AZB

Crystal structure of Escherichia coli Lgt in complex with phosphatidylglycerol and the inhibitor palmitic acid

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 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

223166

PDB entries from 2024-07-31

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