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6VQR

CryoEM Structure of the PfFNT-inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005773cellular_componentvacuole
A0005774cellular_componentvacuolar membrane
A0005886cellular_componentplasma membrane
A0015513molecular_functionhigh-affinity secondary active nitrite transmembrane transporter activity
A0015650molecular_functionlactate:proton symporter activity
A0015706biological_processnitrate transmembrane transport
A0015707biological_processnitrite transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0035873biological_processlactate transmembrane transport
A0055085biological_processtransmembrane transport
B0005773cellular_componentvacuole
B0005774cellular_componentvacuolar membrane
B0005886cellular_componentplasma membrane
B0015513molecular_functionhigh-affinity secondary active nitrite transmembrane transporter activity
B0015650molecular_functionlactate:proton symporter activity
B0015706biological_processnitrate transmembrane transport
B0015707biological_processnitrite transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0035873biological_processlactate transmembrane transport
B0055085biological_processtransmembrane transport
C0005773cellular_componentvacuole
C0005774cellular_componentvacuolar membrane
C0005886cellular_componentplasma membrane
C0015513molecular_functionhigh-affinity secondary active nitrite transmembrane transporter activity
C0015650molecular_functionlactate:proton symporter activity
C0015706biological_processnitrate transmembrane transport
C0015707biological_processnitrite transport
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0035873biological_processlactate transmembrane transport
C0055085biological_processtransmembrane transport
D0005773cellular_componentvacuole
D0005774cellular_componentvacuolar membrane
D0005886cellular_componentplasma membrane
D0015513molecular_functionhigh-affinity secondary active nitrite transmembrane transporter activity
D0015650molecular_functionlactate:proton symporter activity
D0015706biological_processnitrate transmembrane transport
D0015707biological_processnitrite transport
D0016020cellular_componentmembrane
D0022857molecular_functiontransmembrane transporter activity
D0035873biological_processlactate transmembrane transport
D0055085biological_processtransmembrane transport
E0005773cellular_componentvacuole
E0005774cellular_componentvacuolar membrane
E0005886cellular_componentplasma membrane
E0015513molecular_functionhigh-affinity secondary active nitrite transmembrane transporter activity
E0015650molecular_functionlactate:proton symporter activity
E0015706biological_processnitrate transmembrane transport
E0015707biological_processnitrite transport
E0016020cellular_componentmembrane
E0022857molecular_functiontransmembrane transporter activity
E0035873biological_processlactate transmembrane transport
E0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue R7M A 401
ChainResidue
APHE90
AALA93
APHE94
AILE97
ALEU104
ATHR106
AGLY107
AVAL196
AHIS230

site_idAC2
Number of Residues10
Detailsbinding site for residue R7M B 401
ChainResidue
BVAL54
BPHE90
BALA93
BPHE94
BILE97
BLEU104
BTHR106
BGLY107
BVAL196
BHIS230

site_idAC3
Number of Residues7
Detailsbinding site for residue R7M C 401
ChainResidue
CVAL54
CPHE94
CILE97
CLEU104
CGLY107
CVAL196
CHIS230

site_idAC4
Number of Residues11
Detailsbinding site for residue R7M D 401
ChainResidue
DPHE90
DALA93
DPHE94
DILE97
DLEU104
DTHR106
DGLY107
DVAL196
DVAL200
DVAL220
DHIS230

site_idAC5
Number of Residues11
Detailsbinding site for residue R7M E 401
ChainResidue
EPHE94
EILE97
EILE98
ESER102
EASP103
ELEU104
ETHR106
EGLY107
EVAL196
EVAL220
EHIS230

Functional Information from PROSITE/UniProt
site_idPS01006
Number of Residues11
DetailsFORMATE_NITRITE_TP_2 Formate and nitrite transporters signature 2. AvgCNIFVCLA
ChainResidueDetails
AALA189-ALA199

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues365
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-CYS19
BTYR281-ASN309
CMET1-CYS19
CALA36-ASN40
CGLY101-LYS122
CLYS207-GLY209
CTYR281-ASN309
DMET1-CYS19
DALA36-ASN40
DGLY101-LYS122
DLYS207-GLY209
AALA36-ASN40
DTYR281-ASN309
EMET1-CYS19
EALA36-ASN40
EGLY101-LYS122
ELYS207-GLY209
ETYR281-ASN309
AGLY101-LYS122
ALYS207-GLY209
ATYR281-ASN309
BMET1-CYS19
BALA36-ASN40
BGLY101-LYS122
BLYS207-GLY209

site_idSWS_FT_FI2
Number of Residues150
DetailsINTRAMEM: Helical => ECO:0000269|PubMed:33471955, ECO:0007744|PDB:6VQQ, ECO:0007744|PDB:6VQR, ECO:0007744|PDB:7MXY
ChainResidueDetails
AGLY20-LYS35
EASN164-HIS179
AASN164-HIS179
BGLY20-LYS35
BASN164-HIS179
CGLY20-LYS35
CASN164-HIS179
DGLY20-LYS35
DASN164-HIS179
EGLY20-LYS35

site_idSWS_FT_FI3
Number of Residues720
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:33471955, ECO:0000269|PubMed:34499638, ECO:0007744|PDB:6VQQ, ECO:0007744|PDB:6VQR, ECO:0007744|PDB:7E26, ECO:0007744|PDB:7E27, ECO:0007744|PDB:7MXY
ChainResidueDetails
ALEU41-PHE68
BPHE182-LEU206
BALA210-ALA226
BVAL250-ILE280
CLEU41-PHE68
CSER80-THR100
CLEU123-TYR150
CPHE182-LEU206
CALA210-ALA226
CVAL250-ILE280
DLEU41-PHE68
ASER80-THR100
DSER80-THR100
DLEU123-TYR150
DPHE182-LEU206
DALA210-ALA226
DVAL250-ILE280
ELEU41-PHE68
ESER80-THR100
ELEU123-TYR150
EPHE182-LEU206
EALA210-ALA226
ALEU123-TYR150
EVAL250-ILE280
APHE182-LEU206
AALA210-ALA226
AVAL250-ILE280
BLEU41-PHE68
BSER80-THR100
BLEU123-TYR150

site_idSWS_FT_FI4
Number of Residues225
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
ATYR69-ALA79
CLEU151-LYS163
CHIS180-THR181
CGLY227-THR249
DTYR69-ALA79
DLEU151-LYS163
DHIS180-THR181
DGLY227-THR249
ETYR69-ALA79
ELEU151-LYS163
EHIS180-THR181
ALEU151-LYS163
EGLY227-THR249
AHIS180-THR181
AGLY227-THR249
BTYR69-ALA79
BLEU151-LYS163
BHIS180-THR181
BGLY227-THR249
CTYR69-ALA79

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PDB entries from 2025-06-18

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