6BMI
Crystal Structure of GltPh R397C in complex with L-Serine
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 | 0006835 | biological_process | dicarboxylic acid transport |
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 | 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 | 0006835 | biological_process | dicarboxylic acid transport |
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 | 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 | 0006835 | biological_process | dicarboxylic acid transport |
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 | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue NA A 501 |
Chain | Residue |
A | GLY306 |
A | ALA307 |
A | ASN310 |
A | ASN401 |
A | ASP405 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue SER A 502 |
Chain | Residue |
A | THR398 |
A | ASN401 |
A | ARG276 |
A | SER278 |
A | THR314 |
A | ASP394 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue NA B 501 |
Chain | Residue |
B | GLY306 |
B | ALA307 |
B | ASN310 |
B | ASN401 |
B | ASP405 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SER B 502 |
Chain | Residue |
B | ARG276 |
B | SER278 |
B | THR314 |
B | ASP394 |
B | THR398 |
B | ASN401 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA C 501 |
Chain | Residue |
C | SER278 |
C | GLY306 |
C | ALA307 |
C | ASN310 |
C | ASN401 |
C | ASP405 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue NA C 502 |
Chain | Residue |
C | THR308 |
C | SER349 |
C | ILE350 |
C | THR352 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue SER C 503 |
Chain | Residue |
C | ARG276 |
C | SER278 |
C | THR314 |
C | ASP394 |
C | THR398 |
C | ASN401 |
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 | 54 |
Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 216 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 60 |
Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 201 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 66 |
Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 114 |
Details | Transmembrane: {"description":"Discontinuously helical; Name=4","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 63 |
Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 60 |
Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 118 |
Details | Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 66 |
Details | Transmembrane: {"description":"Discontinuously helical; Name=7","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 60 |
Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI12 |
Number of Residues | 13 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2NWL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KBC","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI13 |
Number of Residues | 13 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI14 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X2S","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |