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6BMI

Crystal Structure of GltPh R397C in complex with L-Serine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005283molecular_functionamino acid:sodium symporter activity
A0005886cellular_componentplasma membrane
A0006835biological_processdicarboxylic acid transport
A0006865biological_processamino acid transport
A0015108molecular_functionchloride transmembrane transporter activity
A0015183molecular_functionL-aspartate transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015501molecular_functionglutamate:sodium symporter activity
A0016020cellular_componentmembrane
A0035725biological_processsodium ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070207biological_processprotein homotrimerization
A0070778biological_processL-aspartate transmembrane transport
A0140009biological_processL-aspartate import across plasma membrane
A1902476biological_processchloride transmembrane transport
B0005283molecular_functionamino acid:sodium symporter activity
B0005886cellular_componentplasma membrane
B0006835biological_processdicarboxylic acid transport
B0006865biological_processamino acid transport
B0015108molecular_functionchloride transmembrane transporter activity
B0015183molecular_functionL-aspartate transmembrane transporter activity
B0015293molecular_functionsymporter activity
B0015501molecular_functionglutamate:sodium symporter activity
B0016020cellular_componentmembrane
B0035725biological_processsodium ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0070207biological_processprotein homotrimerization
B0070778biological_processL-aspartate transmembrane transport
B0140009biological_processL-aspartate import across plasma membrane
B1902476biological_processchloride transmembrane transport
C0005283molecular_functionamino acid:sodium symporter activity
C0005886cellular_componentplasma membrane
C0006835biological_processdicarboxylic acid transport
C0006865biological_processamino acid transport
C0015108molecular_functionchloride transmembrane transporter activity
C0015183molecular_functionL-aspartate transmembrane transporter activity
C0015293molecular_functionsymporter activity
C0015501molecular_functionglutamate:sodium symporter activity
C0016020cellular_componentmembrane
C0035725biological_processsodium ion transmembrane transport
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0070207biological_processprotein homotrimerization
C0070778biological_processL-aspartate transmembrane transport
C0140009biological_processL-aspartate import across plasma membrane
C1902476biological_processchloride transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue NA A 501
ChainResidue
AGLY306
AALA307
AASN310
AASN401
AASP405

site_idAC2
Number of Residues6
Detailsbinding site for residue SER A 502
ChainResidue
ATHR398
AASN401
AARG276
ASER278
ATHR314
AASP394

site_idAC3
Number of Residues5
Detailsbinding site for residue NA B 501
ChainResidue
BGLY306
BALA307
BASN310
BASN401
BASP405

site_idAC4
Number of Residues6
Detailsbinding site for residue SER B 502
ChainResidue
BARG276
BSER278
BTHR314
BASP394
BTHR398
BASN401

site_idAC5
Number of Residues6
Detailsbinding site for residue NA C 501
ChainResidue
CSER278
CGLY306
CALA307
CASN310
CASN401
CASP405

site_idAC6
Number of Residues4
Detailsbinding site for residue NA C 502
ChainResidue
CTHR308
CSER349
CILE350
CTHR352

site_idAC7
Number of Residues6
Detailsbinding site for residue SER C 503
ChainResidue
CARG276
CSER278
CTHR314
CASP394
CTHR398
CASN401

Functional Information from PROSITE/UniProt
site_idPS00713
Number of Residues16
DetailsNA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. PfGDlFVrLLKMLVmP
ChainResidueDetails
APRO45-PRO60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues216
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues201
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues66
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues114
DetailsTransmembrane: {"description":"Discontinuously helical; Name=4","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues118
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues66
DetailsTransmembrane: {"description":"Discontinuously helical; Name=7","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues13
DetailsBinding 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"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4X2S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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