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4U4W

Structure of a nitrate/nitrite antiporter NarK in nitrate-bound occluded state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005452molecular_functionsolute:inorganic anion antiporter activity
A0005886cellular_componentplasma membrane
A0015112molecular_functionnitrate transmembrane transporter activity
A0015113molecular_functionnitrite transmembrane transporter activity
A0015706biological_processnitrate transmembrane transport
A0015707biological_processnitrite transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0042128biological_processnitrate assimilation
A0043602biological_processnitrate catabolic process
A0055085biological_processtransmembrane transport
B0005452molecular_functionsolute:inorganic anion antiporter activity
B0005886cellular_componentplasma membrane
B0015112molecular_functionnitrate transmembrane transporter activity
B0015113molecular_functionnitrite transmembrane transporter activity
B0015706biological_processnitrate transmembrane transport
B0015707biological_processnitrite transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0042128biological_processnitrate assimilation
B0043602biological_processnitrate catabolic process
B0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue NO3 A 501
ChainResidue
APHE49
AARG89
APHE147
AASN175
ATYR263
APHE267
AARG305
ASER411

site_idAC2
Number of Residues3
Detailsbinding site for residue OLA A 502
ChainResidue
ATYR92
AOLC509
APRO91

site_idAC3
Number of Residues4
Detailsbinding site for residue OLA A 503
ChainResidue
APRO43
ALEU47
AILE218
APHE222

site_idAC4
Number of Residues3
Detailsbinding site for residue OLA A 504
ChainResidue
APHE121
APHE197
APRO221

site_idAC5
Number of Residues5
Detailsbinding site for residue OLA A 505
ChainResidue
ALEU88
ASER131
ALEU138
APHE142
BOLA502

site_idAC6
Number of Residues4
Detailsbinding site for residue OLA A 506
ChainResidue
APHE420
AALA424
AGLY437
BLYS203

site_idAC7
Number of Residues2
Detailsbinding site for residue OLC A 507
ChainResidue
ALEU183
AGLN292

site_idAC8
Number of Residues8
Detailsbinding site for residue OLC A 508
ChainResidue
APHE107
AGLY110
AILE228
ATRP231
APHE232
AOLC509
BILE228
BPHE232

site_idAC9
Number of Residues7
Detailsbinding site for residue OLC A 509
ChainResidue
AILE98
APHE99
AOLA502
AOLC508
BTRP39
BOLA505
BOLA506

site_idAD1
Number of Residues6
Detailsbinding site for residue NO3 B 501
ChainResidue
BPHE49
BARG89
BPHE147
BASN175
BTYR263
BPHE267

site_idAD2
Number of Residues5
Detailsbinding site for residue OLA B 502
ChainResidue
AILE135
AOLA505
BLEU187
BLEU191
BOLA503

site_idAD3
Number of Residues4
Detailsbinding site for residue OLA B 503
ChainResidue
BLEU47
BTRP219
BPHE222
BOLA502

site_idAD4
Number of Residues3
Detailsbinding site for residue OLA B 504
ChainResidue
BPHE194
BPHE197
BTRP217

site_idAD5
Number of Residues4
Detailsbinding site for residue OLA B 505
ChainResidue
AOLC509
BSER35
BTRP39
BALA166

site_idAD6
Number of Residues2
Detailsbinding site for residue OLA B 506
ChainResidue
AOLC509
BSER306

site_idAD7
Number of Residues15
Detailsbinding site for residue OLC B 507
ChainResidue
AILE111
ATRP118
APHE121
AASP125
ALEU139
APHE142
BSER192
BILE193
BPHE194
BALA195
BVAL196
BILE218
BPHE222
BILE225
BHOH645

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues218
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V
ChainResidueDetails
AMET1-ASN37
BMET234-ARG253
BASP313-GLY316
BSER374-ALA405
AVAL96-ARG102
AALA152-ALA166
AMET234-ARG253
AASP313-GLY316
ASER374-ALA405
BMET1-ASN37
BVAL96-ARG102
BALA152-ALA166

site_idSWS_FT_FI2
Number of Residues524
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V
ChainResidueDetails
ALEU38-ALA59
APHE348-ILE373
AALA406-SER427
AVAL436-GLY458
BLEU38-ALA59
BLEU74-MET95
BARG103-ALA122
BSER131-MET151
BLEU167-VAL189
BLEU212-GLY233
BGLY254-SER281
ALEU74-MET95
BILE290-SER312
BGLY317-THR338
BPHE348-ILE373
BALA406-SER427
BVAL436-GLY458
AARG103-ALA122
ASER131-MET151
ALEU167-VAL189
ALEU212-GLY233
AGLY254-SER281
AILE290-SER312
AGLY317-THR338

site_idSWS_FT_FI3
Number of Residues126
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V
ChainResidueDetails
AVAL60-GLN73
BLYS282-GLN289
BLEU339-SER347
BSER428-PRO435
AVAL123-TYR130
ASER190-TYR211
ALYS282-GLN289
ALEU339-SER347
ASER428-PRO435
BVAL60-GLN73
BVAL123-TYR130
BSER190-TYR211

site_idSWS_FT_FI4
Number of Residues8
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4V
ChainResidueDetails
AARG459-LYS463
BARG459-LYS463

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:23665960, ECO:0007744|PDB:4JRE
ChainResidueDetails
AARG89
ATYR263
BARG89
BTYR263

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T, ECO:0007744|PDB:4U4W
ChainResidueDetails
AASN175
BASN175

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:25959928, ECO:0007744|PDB:4U4T
ChainResidueDetails
ASER411
BSER411

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Important for activity => ECO:0000305|PubMed:23665960, ECO:0000305|PubMed:25959928
ChainResidueDetails
AARG305
BARG305

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PDB entries from 2024-07-24

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