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5CFY

CRYSTAL STRUCTURE OF GLTPH R397A IN COMPLEX WITH NA+ AND L-ASP

Replaces:  4OYG
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
D0005283molecular_functionamino acid:sodium symporter activity
D0005886cellular_componentplasma membrane
D0006835biological_processdicarboxylic acid transport
D0006865biological_processamino acid transport
D0015108molecular_functionchloride transmembrane transporter activity
D0015183molecular_functionL-aspartate transmembrane transporter activity
D0015293molecular_functionsymporter activity
D0015501molecular_functionglutamate:sodium symporter activity
D0016020cellular_componentmembrane
D0035725biological_processsodium ion transmembrane transport
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0070207biological_processprotein homotrimerization
D0070778biological_processL-aspartate transmembrane transport
D0140009biological_processL-aspartate import across plasma membrane
D1902476biological_processchloride transmembrane transport
E0005283molecular_functionamino acid:sodium symporter activity
E0005886cellular_componentplasma membrane
E0006835biological_processdicarboxylic acid transport
E0006865biological_processamino acid transport
E0015108molecular_functionchloride transmembrane transporter activity
E0015183molecular_functionL-aspartate transmembrane transporter activity
E0015293molecular_functionsymporter activity
E0015501molecular_functionglutamate:sodium symporter activity
E0016020cellular_componentmembrane
E0035725biological_processsodium ion transmembrane transport
E0042802molecular_functionidentical protein binding
E0046872molecular_functionmetal ion binding
E0070207biological_processprotein homotrimerization
E0070778biological_processL-aspartate transmembrane transport
E0140009biological_processL-aspartate import across plasma membrane
E1902476biological_processchloride transmembrane transport
F0005283molecular_functionamino acid:sodium symporter activity
F0005886cellular_componentplasma membrane
F0006835biological_processdicarboxylic acid transport
F0006865biological_processamino acid transport
F0015108molecular_functionchloride transmembrane transporter activity
F0015183molecular_functionL-aspartate transmembrane transporter activity
F0015293molecular_functionsymporter activity
F0015501molecular_functionglutamate:sodium symporter activity
F0016020cellular_componentmembrane
F0035725biological_processsodium ion transmembrane transport
F0042802molecular_functionidentical protein binding
F0046872molecular_functionmetal ion binding
F0070207biological_processprotein homotrimerization
F0070778biological_processL-aspartate transmembrane transport
F0140009biological_processL-aspartate import across plasma membrane
F1902476biological_processchloride transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue ASP A 501
ChainResidue
AARG276
AGLY359
AASP394
ATHR398
AASN401
ASER277
ASER278
AMET311
ATHR314
ATYR317
AGLY354
AVAL355
AGLY357

site_idAC2
Number of Residues6
Detailsbinding site for residue NA A 502
ChainResidue
ATHR308
AMET311
ASER349
AILE350
AGLY351
ATHR352

site_idAC3
Number of Residues6
Detailsbinding site for residue NA A 503
ChainResidue
ASER278
AGLY306
AALA307
AASN310
AASN401
AASP405

site_idAC4
Number of Residues15
Detailsbinding site for residue ASP B 501
ChainResidue
BARG276
BSER277
BSER278
BMET311
BTHR314
BTYR317
BTHR352
BGLY354
BVAL355
BPRO356
BGLY357
BGLY359
BASP394
BTHR398
BASN401

site_idAC5
Number of Residues5
Detailsbinding site for residue NA B 502
ChainResidue
BTHR308
BMET311
BSER349
BILE350
BTHR352

site_idAC6
Number of Residues6
Detailsbinding site for residue NA B 503
ChainResidue
BSER278
BGLY306
BALA307
BASN310
BASN401
BASP405

site_idAC7
Number of Residues15
Detailsbinding site for residue ASP C 501
ChainResidue
CARG276
CSER277
CSER278
CMET311
CTHR314
CTYR317
CGLY354
CVAL355
CPRO356
CGLY357
CALA358
CGLY359
CASP394
CTHR398
CASN401

site_idAC8
Number of Residues6
Detailsbinding site for residue NA C 502
ChainResidue
CTHR308
CMET311
CSER349
CILE350
CGLY351
CTHR352

site_idAC9
Number of Residues6
Detailsbinding site for residue NA C 503
ChainResidue
CSER278
CGLY306
CALA307
CASN310
CASN401
CASP405

site_idAD1
Number of Residues15
Detailsbinding site for residue ASP D 501
ChainResidue
DARG276
DSER277
DSER278
DMET311
DTHR314
DTYR317
DGLY354
DVAL355
DPRO356
DGLY357
DALA358
DGLY359
DASP394
DTHR398
DASN401

site_idAD2
Number of Residues6
Detailsbinding site for residue NA D 502
ChainResidue
DTHR308
DMET311
DSER349
DILE350
DGLY351
DTHR352

site_idAD3
Number of Residues6
Detailsbinding site for residue NA D 503
ChainResidue
DSER278
DGLY306
DALA307
DASN310
DASN401
DASP405

site_idAD4
Number of Residues13
Detailsbinding site for residue ASP E 501
ChainResidue
EARG276
ESER277
ESER278
EMET311
ETHR314
ETYR317
EGLY354
EGLY357
EALA358
EGLY359
EASP394
ETHR398
EASN401

site_idAD5
Number of Residues6
Detailsbinding site for residue NA E 502
ChainResidue
ETHR308
EMET311
ESER349
EILE350
EGLY351
ETHR352

site_idAD6
Number of Residues6
Detailsbinding site for residue NA E 503
ChainResidue
ESER278
EGLY306
EALA307
EASN310
EASN401
EASP405

site_idAD7
Number of Residues15
Detailsbinding site for residue ASP F 501
ChainResidue
FARG276
FSER277
FSER278
FMET311
FTHR314
FTYR317
FTHR352
FGLY354
FVAL355
FPRO356
FGLY357
FGLY359
FASP394
FTHR398
FASN401

site_idAD8
Number of Residues5
Detailsbinding site for residue NA F 502
ChainResidue
FTHR308
FMET311
FSER349
FILE350
FTHR352

site_idAD9
Number of Residues6
Detailsbinding site for residue NA F 503
ChainResidue
FSER278
FGLY306
FALA307
FASN310
FASN401
FASP405

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 Residues108
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues432
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues120
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues402
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues132
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues228
DetailsTransmembrane: {"description":"Discontinuously helical; Name=4","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues126
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues120
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues372
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues132
DetailsTransmembrane: {"description":"Discontinuously helical; Name=7","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues120
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"15483603","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues30
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 Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17230192","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2NWX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
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

246704

PDB entries from 2025-12-24

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