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4C7R

Inward facing conformation of the trimeric betaine transporter BetP in complex with lipids

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0015293molecular_functionsymporter activity
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0071705biological_processnitrogen compound transport
B0005886cellular_componentplasma membrane
B0015293molecular_functionsymporter activity
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0055085biological_processtransmembrane transport
B0071705biological_processnitrogen compound transport
C0005886cellular_componentplasma membrane
C0015293molecular_functionsymporter activity
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0055085biological_processtransmembrane transport
C0071705biological_processnitrogen compound transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FLC A 1001
ChainResidue
AALA148
AGLY149
AGLY151
ATRP377
APHE380

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FLC B 1001
ChainResidue
BTRP377
BALA147
BALA148
BGLY149
BMET150

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FLC C 1001
ChainResidue
CALA148
CMET150
CTRP377
CPHE380
CHOH2006
CHOH2014
CHOH2020

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL C 1562
ChainResidue
CARG126
CASP131
CARG210
CILE549

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 1553
ChainResidue
BARG126
BARG210

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 1587
ChainResidue
AASN177
AGLY179
BALA355

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL C 1563
ChainResidue
BGLY179
CALA355

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1564
ChainResidue
AALA355
CASN177
CGLY179

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGT A 1588
ChainResidue
AALA119
ALEU399
APGT1589
APGT1591
APGT1592
BSER120
BLYS121
BPGT1554

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGT B 1554
ChainResidue
APGT1588
APGT1592
BPHE112
BPHE113
BALA119
BVAL541
BTYR550

site_idBC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PGT A 1589
ChainResidue
APHE112
ASER120
ALYS121
APGT1588
APGT1590
APGT1591
APGT1592
CSER120
CLYS121
CLEU191
CARG395
CLEU399
CLEU403

site_idBC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGT C 1565
ChainResidue
CSER143
CMET150
CMET310
CVAL311
CALA313
CALA314
CILE318
CPGT1566

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PGT C 1566
ChainResidue
AASN98
CVAL322
CVAL323
CGLY324
CTHR326
CPGT1565

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PGT A 1590
ChainResidue
AVAL116
AARG554
AARG558
APGT1589
CARG126
CSER393
CARG395
CGLU396

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PGT A 1591
ChainResidue
APHE345
APGT1588
APGT1589
BPHE345
CLEU341

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PGT A 1592
ChainResidue
APGT1588
APGT1589
BALA118
BALA119
BARG395
BPGT1554
CTYR550

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PGT C 1567
ChainResidue
CPHE538
CVAL541
CLYS542
CCM51568

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CM5 C 1568
ChainResidue
CILE238
CPGT1567
CILE225
CLYS228

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FLC C 1569
ChainResidue
CARG167
CASN168
CGLU175

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 1555
ChainResidue
BSER306
BPHE384
BTHR467
BSER471

Functional Information from PROSITE/UniProt
site_idPS01303
Number of Residues10
DetailsBCCT BCCT family of transporters signature. SWTIfYWaWW
ChainResidueDetails
ASER365-TRP374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues738
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24141878","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues432
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues207
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25023443","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AIN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19262666","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22940865","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4AIN","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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