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9BIS

Cryo-EM structure of the mammalian peptide transporter PepT2 bound to amoxicillin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006857biological_processoligopeptide transport
A0015031biological_processprotein transport
A0015293molecular_functionsymporter activity
A0015333molecular_functionpeptide:proton symporter activity
A0015334molecular_functionhigh-affinity oligopeptide transmembrane transporter activity
A0015833biological_processpeptide transport
A0015835biological_processpeptidoglycan transport
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0030670cellular_componentphagocytic vesicle membrane
A0031410cellular_componentcytoplasmic vesicle
A0042908biological_processxenobiotic transport
A0042937molecular_functiontripeptide transmembrane transporter activity
A0042938biological_processdipeptide transport
A0045087biological_processinnate immune response
A0070293biological_processrenal absorption
A0070424biological_processregulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway
A0071916molecular_functiondipeptide transmembrane transporter activity
A0072237biological_processmetanephric proximal tubule development
A0140206biological_processdipeptide import across plasma membrane
A0140207biological_processtripeptide import across plasma membrane
A0140367biological_processantibacterial innate immune response
A1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS01022
Number of Residues25
DetailsPTR2_1 PTR2 family proton/oligopeptide symporters signature 1. GAAIADsWLGkfkTIiylSlVyvlG
ChainResidueDetails
AGLY100-GLY124

site_idPS01023
Number of Residues13
DetailsPTR2_2 PTR2 family proton/oligopeptide symporters signature 2. FsvFYLaINAGSL
ChainResidueDetails
APHE184-LEU196

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues196
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-ARG57
AGLY109-THR113
ALYS161-TYR183
ASER239-ASP295
AARG365-MET380
ASER633-SER643
ATYR696-LEU729

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
APHE58-ASN78
ALEU612-PHE632
AVAL644-ALA664
APHE675-TYR695
AALA88-LEU108
AILE114-PRO134
AMET140-ILE160
APHE184-MET204
AALA218-GLY238
AVAL296-LEU316
AMET344-TYR364
AALA381-ILE401

site_idSWS_FT_FI3
Number of Residues268
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AGLU79-HIS87
AILE135-LYS139
ALEU205-TYR217
AASP317-GLN343
AASN402-GLN611
AGLN665-GLU674

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9ES07
ChainResidueDetails
ASER9

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9ES07
ChainResidueDetails
ATHR12

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER28

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN435
AASN448
AASN528

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN587

226707

PDB entries from 2024-10-30

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