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8FHT

Cryo-EM structure of human NCC

Functional Information from GO Data
ChainGOidnamespacecontents
A0002021biological_processresponse to dietary excess
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0006884biological_processcell volume homeostasis
A0007165biological_processsignal transduction
A0008511molecular_functionsodium:potassium:chloride symporter activity
A0015081molecular_functionsodium ion transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015377molecular_functionchloride:monoatomic cation symporter activity
A0015378molecular_functionsodium:chloride symporter activity
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0022857molecular_functiontransmembrane transporter activity
A0035725biological_processsodium ion transmembrane transport
A0046873molecular_functionmetal ion transmembrane transporter activity
A0055064biological_processchloride ion homeostasis
A0055075biological_processpotassium ion homeostasis
A0055078biological_processsodium ion homeostasis
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0070294biological_processrenal sodium ion absorption
A0071241biological_processobsolete cellular response to inorganic substance
A1902476biological_processchloride transmembrane transport
A1904044biological_processresponse to aldosterone
A1990573biological_processpotassium ion import across plasma membrane
B0002021biological_processresponse to dietary excess
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006814biological_processsodium ion transport
B0006884biological_processcell volume homeostasis
B0007165biological_processsignal transduction
B0008511molecular_functionsodium:potassium:chloride symporter activity
B0015081molecular_functionsodium ion transmembrane transporter activity
B0015293molecular_functionsymporter activity
B0015377molecular_functionchloride:monoatomic cation symporter activity
B0015378molecular_functionsodium:chloride symporter activity
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0022857molecular_functiontransmembrane transporter activity
B0035725biological_processsodium ion transmembrane transport
B0046873molecular_functionmetal ion transmembrane transporter activity
B0055064biological_processchloride ion homeostasis
B0055075biological_processpotassium ion homeostasis
B0055078biological_processsodium ion homeostasis
B0055085biological_processtransmembrane transport
B0070062cellular_componentextracellular exosome
B0070294biological_processrenal sodium ion absorption
B0071241biological_processobsolete cellular response to inorganic substance
B1902476biological_processchloride transmembrane transport
B1904044biological_processresponse to aldosterone
B1990573biological_processpotassium ion import across plasma membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1206
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:36351028, ECO:0000269|PubMed:36792826, ECO:0007744|PDB:7Y6I, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR, ECO:0007744|PDB:8FHT
ChainResidueDetails
AMET1-GLY137
BGLY278
BSER361-ASP366
BASP486-PRO505
BSER555-TYR565
BLYS607-GLN1021
ATHR194-GLY212
AGLY278
ASER361-ASP366
AASP486-PRO505
ASER555-TYR565
ALYS607-GLN1021
BMET1-GLY137
BTHR194-GLY212

site_idSWS_FT_FI2
Number of Residues56
DetailsTRANSMEM: Discontinuously helical => ECO:0000269|PubMed:36351028, ECO:0000269|PubMed:36792826, ECO:0007744|PDB:7Y6I, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR, ECO:0007744|PDB:8FHT
ChainResidueDetails
ATRP138-ALA166
BTRP138-ALA166

site_idSWS_FT_FI3
Number of Residues198
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:36351028, ECO:0000269|PubMed:36792826, ECO:0007744|PDB:7Y6I, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR, ECO:0007744|PDB:8FHT
ChainResidueDetails
AGLY167
BVAL397-PHE453
BGLU524-LEU525
BTHR585
AGLY250-ILE257
AILE306-THR339
AVAL397-PHE453
AGLU524-LEU525
ATHR585
BGLY167
BGLY250-ILE257
BILE306-THR339

site_idSWS_FT_FI4
Number of Residues538
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:36351028, ECO:0000269|PubMed:36792826, ECO:0007744|PDB:7Y6I, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR, ECO:0007744|PDB:8FHT
ChainResidueDetails
AILE168-SER193
AASN566-LEU584
ATRP586-LYS606
BILE168-SER193
BPRO213-TYR249
BASN258-ALA277
BMET279-LEU305
BPHE340-ILE360
BPRO367-CYS396
BALA454-GLU485
BVAL506-ALA523
APRO213-TYR249
BASN526-ASN554
BASN566-LEU584
BTRP586-LYS606
AASN258-ALA277
AMET279-LEU305
APHE340-ILE360
APRO367-CYS396
AALA454-GLU485
AVAL506-ALA523
AASN526-ASN554

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:36351028, ECO:0000269|PubMed:36792826, ECO:0007744|PDB:7Y6I, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR, ECO:0007744|PDB:8FHT
ChainResidueDetails
ALEU148
BSER468
ATRP151
AALA464
ASER467
ASER468
BLEU148
BTRP151
BALA464
BSER467

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR
ChainResidueDetails
AASN149
BASN149

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ
ChainResidueDetails
AASN227
BASN227

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHQ, ECO:0007744|PDB:8FHR
ChainResidueDetails
AHIS234
BHIS234

site_idSWS_FT_FI9
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHP, ECO:0007744|PDB:8FHR
ChainResidueDetails
ATHR352
BTHR352

site_idSWS_FT_FI10
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:36351028, ECO:0000305|PubMed:36792826
ChainResidueDetails
AGLY353
AILE354
ALEU355
ATYR540
BGLY353
BILE354
BLEU355
BTYR540

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHN
ChainResidueDetails
AASN359
BASN359

site_idSWS_FT_FI12
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:36792826, ECO:0007744|PDB:8FHN, ECO:0007744|PDB:8FHO
ChainResidueDetails
ALEU648
BGLY741
BLEU780
BASN781
AARG655
AVAL677
AGLY741
ALEU780
AASN781
BLEU648
BARG655
BVAL677

site_idSWS_FT_FI13
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P59158
ChainResidueDetails
ASER43
ASER49
AASP73
ASER126
BSER43
BSER49
BASP73
BSER126

site_idSWS_FT_FI14
Number of Residues6
DetailsMOD_RES: Phosphothreonine; by OXSR1 and STK39 => ECO:0000269|PubMed:18270262
ChainResidueDetails
ATHR46
AASP55
AASP60
BTHR46
BASP55
BASP60

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P59158
ChainResidueDetails
ATHR50
ATHR124
BTHR50
BTHR124

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine; by OXSR1 and STK39 => ECO:0000305|PubMed:18270262, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER91
BSER91

site_idSWS_FT_FI17
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:36351028, ECO:0007744|PDB:7Y6I
ChainResidueDetails
AASN406
AASN426
BASN406
BASN426

222415

PDB entries from 2024-07-10

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