3V8G
Crystal structure of an asymmetric trimer of a glutamate transporter homologue (GltPh)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005283 | molecular_function | amino acid:sodium symporter activity |
A | 0005886 | cellular_component | plasma membrane |
A | 0006865 | biological_process | amino acid transport |
A | 0015108 | molecular_function | chloride transmembrane transporter activity |
A | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
A | 0015293 | molecular_function | symporter activity |
A | 0015501 | molecular_function | glutamate:sodium symporter activity |
A | 0016020 | cellular_component | membrane |
A | 0035725 | biological_process | sodium ion transmembrane transport |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0046942 | biological_process | carboxylic acid transport |
A | 0070207 | biological_process | protein homotrimerization |
A | 0070778 | biological_process | L-aspartate transmembrane transport |
A | 0140009 | biological_process | L-aspartate import across plasma membrane |
A | 1902476 | biological_process | chloride transmembrane transport |
B | 0005283 | molecular_function | amino acid:sodium symporter activity |
B | 0005886 | cellular_component | plasma membrane |
B | 0006865 | biological_process | amino acid transport |
B | 0015108 | molecular_function | chloride transmembrane transporter activity |
B | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
B | 0015293 | molecular_function | symporter activity |
B | 0015501 | molecular_function | glutamate:sodium symporter activity |
B | 0016020 | cellular_component | membrane |
B | 0035725 | biological_process | sodium ion transmembrane transport |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0046942 | biological_process | carboxylic acid transport |
B | 0070207 | biological_process | protein homotrimerization |
B | 0070778 | biological_process | L-aspartate transmembrane transport |
B | 0140009 | biological_process | L-aspartate import across plasma membrane |
B | 1902476 | biological_process | chloride transmembrane transport |
C | 0005283 | molecular_function | amino acid:sodium symporter activity |
C | 0005886 | cellular_component | plasma membrane |
C | 0006865 | biological_process | amino acid transport |
C | 0015108 | molecular_function | chloride transmembrane transporter activity |
C | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
C | 0015293 | molecular_function | symporter activity |
C | 0015501 | molecular_function | glutamate:sodium symporter activity |
C | 0016020 | cellular_component | membrane |
C | 0035725 | biological_process | sodium ion transmembrane transport |
C | 0042802 | molecular_function | identical protein binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0046942 | biological_process | carboxylic acid transport |
C | 0070207 | biological_process | protein homotrimerization |
C | 0070778 | biological_process | L-aspartate transmembrane transport |
C | 0140009 | biological_process | L-aspartate import across plasma membrane |
C | 1902476 | biological_process | chloride transmembrane transport |
D | 0005283 | molecular_function | amino acid:sodium symporter activity |
D | 0005886 | cellular_component | plasma membrane |
D | 0006865 | biological_process | amino acid transport |
D | 0015108 | molecular_function | chloride transmembrane transporter activity |
D | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
D | 0015293 | molecular_function | symporter activity |
D | 0015501 | molecular_function | glutamate:sodium symporter activity |
D | 0016020 | cellular_component | membrane |
D | 0035725 | biological_process | sodium ion transmembrane transport |
D | 0042802 | molecular_function | identical protein binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0046942 | biological_process | carboxylic acid transport |
D | 0070207 | biological_process | protein homotrimerization |
D | 0070778 | biological_process | L-aspartate transmembrane transport |
D | 0140009 | biological_process | L-aspartate import across plasma membrane |
D | 1902476 | biological_process | chloride transmembrane transport |
E | 0005283 | molecular_function | amino acid:sodium symporter activity |
E | 0005886 | cellular_component | plasma membrane |
E | 0006865 | biological_process | amino acid transport |
E | 0015108 | molecular_function | chloride transmembrane transporter activity |
E | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
E | 0015293 | molecular_function | symporter activity |
E | 0015501 | molecular_function | glutamate:sodium symporter activity |
E | 0016020 | cellular_component | membrane |
E | 0035725 | biological_process | sodium ion transmembrane transport |
E | 0042802 | molecular_function | identical protein binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0046942 | biological_process | carboxylic acid transport |
E | 0070207 | biological_process | protein homotrimerization |
E | 0070778 | biological_process | L-aspartate transmembrane transport |
E | 0140009 | biological_process | L-aspartate import across plasma membrane |
E | 1902476 | biological_process | chloride transmembrane transport |
F | 0005283 | molecular_function | amino acid:sodium symporter activity |
F | 0005886 | cellular_component | plasma membrane |
F | 0006865 | biological_process | amino acid transport |
F | 0015108 | molecular_function | chloride transmembrane transporter activity |
F | 0015183 | molecular_function | L-aspartate transmembrane transporter activity |
F | 0015293 | molecular_function | symporter activity |
F | 0015501 | molecular_function | glutamate:sodium symporter activity |
F | 0016020 | cellular_component | membrane |
F | 0035725 | biological_process | sodium ion transmembrane transport |
F | 0042802 | molecular_function | identical protein binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0046942 | biological_process | carboxylic acid transport |
F | 0070207 | biological_process | protein homotrimerization |
F | 0070778 | biological_process | L-aspartate transmembrane transport |
F | 0140009 | biological_process | L-aspartate import across plasma membrane |
F | 1902476 | biological_process | chloride transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ASP A 501 |
Chain | Residue |
A | ARG276 |
A | GLY359 |
A | ASP394 |
A | ARG397 |
A | THR398 |
A | ASN401 |
A | SER277 |
A | SER278 |
A | MET311 |
A | THR314 |
A | THR352 |
A | GLY354 |
A | VAL355 |
A | PRO356 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 502 |
Chain | Residue |
A | GLY306 |
A | ILE309 |
A | ASN310 |
A | ASN401 |
A | ASP405 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA A 503 |
Chain | Residue |
A | THR308 |
A | MET311 |
A | SER349 |
A | ILE350 |
A | GLY351 |
A | THR352 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ASP B 501 |
Chain | Residue |
B | ARG276 |
B | SER277 |
B | SER278 |
B | MET311 |
B | THR314 |
B | THR352 |
B | GLY354 |
B | VAL355 |
B | PRO356 |
B | GLY359 |
B | ASP394 |
B | ARG397 |
B | THR398 |
B | ASN401 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA B 502 |
Chain | Residue |
B | GLY306 |
B | ILE309 |
B | ASN310 |
B | ASN401 |
B | ASP405 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA B 503 |
Chain | Residue |
B | THR308 |
B | MET311 |
B | SER349 |
B | ILE350 |
B | GLY351 |
B | THR352 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ASP C 501 |
Chain | Residue |
C | ARG276 |
C | SER277 |
C | SER278 |
C | MET311 |
C | GLY354 |
C | VAL355 |
C | PRO356 |
C | ALA358 |
C | GLY359 |
C | ASP394 |
C | ARG397 |
C | THR398 |
C | ASN401 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA C 502 |
Chain | Residue |
C | GLY306 |
C | ASN310 |
C | ASP405 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA C 503 |
Chain | Residue |
C | THR308 |
C | ILE309 |
C | SER349 |
C | ILE350 |
C | THR352 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ASP D 501 |
Chain | Residue |
D | ARG276 |
D | SER277 |
D | SER278 |
D | THR314 |
D | THR352 |
D | GLY354 |
D | VAL355 |
D | PRO356 |
D | GLY359 |
D | ASP394 |
D | ARG397 |
D | THR398 |
D | ASN401 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA D 502 |
Chain | Residue |
D | GLY306 |
D | ILE309 |
D | ASN310 |
D | ASN401 |
D | ASP405 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA D 503 |
Chain | Residue |
D | THR308 |
D | MET311 |
D | SER349 |
D | ILE350 |
D | GLY351 |
D | THR352 |
site_id | BC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ASP E 501 |
Chain | Residue |
E | THR314 |
E | THR352 |
E | GLY354 |
E | VAL355 |
E | PRO356 |
E | GLY359 |
E | ASP394 |
E | ARG397 |
E | THR398 |
E | ASN401 |
E | ARG276 |
E | SER277 |
E | SER278 |
E | MET311 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA E 502 |
Chain | Residue |
E | GLY306 |
E | ILE309 |
E | ASN310 |
E | ASN401 |
E | ASP405 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA E 503 |
Chain | Residue |
E | THR308 |
E | MET311 |
E | SER349 |
E | ILE350 |
E | GLY351 |
E | THR352 |
site_id | BC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE ASP F 501 |
Chain | Residue |
F | ARG276 |
F | SER277 |
F | SER278 |
F | MET311 |
F | GLY354 |
F | VAL355 |
F | PRO356 |
F | ALA358 |
F | GLY359 |
F | ASP394 |
F | ARG397 |
F | THR398 |
F | ASN401 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA F 502 |
Chain | Residue |
F | GLY306 |
F | ASN310 |
F | ASN401 |
F | ASP405 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA F 503 |
Chain | Residue |
F | THR308 |
F | SER349 |
F | ILE350 |
F | THR352 |
Functional Information from PROSITE/UniProt
site_id | PS00713 |
Number of Residues | 16 |
Details | NA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. PfGDlFVrLLKMLVmP |
Chain | Residue | Details |
A | PRO45-PRO60 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 462 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | MET1-PRO11 | |
B | LYS290-GLY297 | |
C | MET1-PRO11 | |
C | PHE63-ARG80 | |
C | LEU161-LYS196 | |
C | LYS252-SER260 | |
C | LYS290-GLY297 | |
D | MET1-PRO11 | |
D | PHE63-ARG80 | |
D | LEU161-LYS196 | |
D | LYS252-SER260 | |
A | PHE63-ARG80 | |
D | LYS290-GLY297 | |
E | MET1-PRO11 | |
E | PHE63-ARG80 | |
E | LEU161-LYS196 | |
E | LYS252-SER260 | |
E | LYS290-GLY297 | |
F | MET1-PRO11 | |
F | PHE63-ARG80 | |
F | LEU161-LYS196 | |
F | LYS252-SER260 | |
A | LEU161-LYS196 | |
F | LYS290-GLY297 | |
A | LYS252-SER260 | |
A | LYS290-GLY297 | |
B | MET1-PRO11 | |
B | PHE63-ARG80 | |
B | LEU161-LYS196 | |
B | LYS252-SER260 |
site_id | SWS_FT_FI2 |
Number of Residues | 108 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | VAL12-LEU30 | |
B | VAL12-LEU30 | |
C | VAL12-LEU30 | |
D | VAL12-LEU30 | |
E | VAL12-LEU30 | |
F | VAL12-LEU30 |
site_id | SWS_FT_FI3 |
Number of Residues | 432 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | GLY31-THR41 | |
B | PRO373-ALA391 | |
C | GLY31-THR41 | |
C | ALA104-GLN121 | |
C | GLU219-LYS230 | |
C | ALA321-GLN337 | |
C | PRO373-ALA391 | |
D | GLY31-THR41 | |
D | ALA104-GLN121 | |
D | GLU219-LYS230 | |
D | ALA321-GLN337 | |
A | ALA104-GLN121 | |
D | PRO373-ALA391 | |
E | GLY31-THR41 | |
E | ALA104-GLN121 | |
E | GLU219-LYS230 | |
E | ALA321-GLN337 | |
E | PRO373-ALA391 | |
F | GLY31-THR41 | |
F | ALA104-GLN121 | |
F | GLU219-LYS230 | |
F | ALA321-GLN337 | |
A | GLU219-LYS230 | |
F | PRO373-ALA391 | |
A | ALA321-GLN337 | |
A | PRO373-ALA391 | |
B | GLY31-THR41 | |
B | ALA104-GLN121 | |
B | GLU219-LYS230 | |
B | ALA321-GLN337 |
site_id | SWS_FT_FI4 |
Number of Residues | 120 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | TYR42-VAL62 | |
B | TYR42-VAL62 | |
C | TYR42-VAL62 | |
D | TYR42-VAL62 | |
E | TYR42-VAL62 | |
F | TYR42-VAL62 |
site_id | SWS_FT_FI5 |
Number of Residues | 132 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | VAL81-MET103 | |
B | VAL81-MET103 | |
C | VAL81-MET103 | |
D | VAL81-MET103 | |
E | VAL81-MET103 | |
F | VAL81-MET103 |
site_id | SWS_FT_FI6 |
Number of Residues | 228 |
Details | TRANSMEM: Discontinuously helical; Name=4 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | PHE122-ILE160 | |
B | PHE122-ILE160 | |
C | PHE122-ILE160 | |
D | PHE122-ILE160 | |
E | PHE122-ILE160 | |
F | PHE122-ILE160 |
site_id | SWS_FT_FI7 |
Number of Residues | 126 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | ILE197-ALA218 | |
B | ILE197-ALA218 | |
C | ILE197-ALA218 | |
D | ILE197-ALA218 | |
E | ILE197-ALA218 | |
F | ILE197-ALA218 |
site_id | SWS_FT_FI8 |
Number of Residues | 120 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | VAL231-LEU251 | |
B | VAL231-LEU251 | |
C | VAL231-LEU251 | |
D | VAL231-LEU251 | |
E | VAL231-LEU251 | |
F | VAL231-LEU251 |
site_id | SWS_FT_FI9 |
Number of Residues | 372 |
Details | INTRAMEM: Discontinuously helical => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | PHE261-ALA289 | |
E | GLN338-LEU372 | |
F | PHE261-ALA289 | |
F | GLN338-LEU372 | |
A | GLN338-LEU372 | |
B | PHE261-ALA289 | |
B | GLN338-LEU372 | |
C | PHE261-ALA289 | |
C | GLN338-LEU372 | |
D | PHE261-ALA289 | |
D | GLN338-LEU372 | |
E | PHE261-ALA289 |
site_id | SWS_FT_FI10 |
Number of Residues | 132 |
Details | TRANSMEM: Discontinuously helical; Name=7 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | ILE298-VAL320 | |
B | ILE298-VAL320 | |
C | ILE298-VAL320 | |
D | ILE298-VAL320 | |
E | ILE298-VAL320 | |
F | ILE298-VAL320 |
site_id | SWS_FT_FI11 |
Number of Residues | 120 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:15483603 |
Chain | Residue | Details |
A | ILE392-VAL412 | |
B | ILE392-VAL412 | |
C | ILE392-VAL412 | |
D | ILE392-VAL412 | |
E | ILE392-VAL412 | |
F | ILE392-VAL412 |
site_id | SWS_FT_FI12 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17230192, ECO:0007744|PDB:2NWL, ECO:0007744|PDB:2NWX, ECO:0007744|PDB:3KBC |
Chain | Residue | Details |
A | ARG276 | |
C | THR314 | |
C | VAL355 | |
C | ASP394 | |
D | ARG276 | |
D | THR314 | |
D | VAL355 | |
D | ASP394 | |
E | ARG276 | |
E | THR314 | |
E | VAL355 | |
A | THR314 | |
E | ASP394 | |
F | ARG276 | |
F | THR314 | |
F | VAL355 | |
F | ASP394 | |
A | VAL355 | |
A | ASP394 | |
B | ARG276 | |
B | THR314 | |
B | VAL355 | |
B | ASP394 | |
C | ARG276 |
site_id | SWS_FT_FI13 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17230192, ECO:0007744|PDB:2NWX |
Chain | Residue | Details |
A | GLY306 | |
B | ASP405 | |
C | GLY306 | |
C | THR308 | |
C | THR352 | |
C | ASN401 | |
C | ASP405 | |
D | GLY306 | |
D | THR308 | |
D | THR352 | |
D | ASN401 | |
A | THR308 | |
D | ASP405 | |
E | GLY306 | |
E | THR308 | |
E | THR352 | |
E | ASN401 | |
E | ASP405 | |
F | GLY306 | |
F | THR308 | |
F | THR352 | |
F | ASN401 | |
A | THR352 | |
F | ASP405 | |
A | ASN401 | |
A | ASP405 | |
B | GLY306 | |
B | THR308 | |
B | THR352 | |
B | ASN401 |
site_id | SWS_FT_FI14 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:17230192, ECO:0007744|PDB:2NWX, ECO:0007744|PDB:4X2S |
Chain | Residue | Details |
A | ASN310 | |
B | ASN310 | |
C | ASN310 | |
D | ASN310 | |
E | ASN310 | |
F | ASN310 |