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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8FHR

Cryo-EM structure of human NCC (class 3-3)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006811	biological_process	monoatomic ion transport
A	0015377	molecular_function	chloride:monoatomic cation symporter activity
A	0016020	cellular_component	membrane
A	0022857	molecular_function	transmembrane transporter activity
A	0055085	biological_process	transmembrane transport
B	0006811	biological_process	monoatomic ion transport
B	0015377	molecular_function	chloride:monoatomic cation symporter activity
B	0016020	cellular_component	membrane
B	0022857	molecular_function	transmembrane transporter activity
B	0055085	biological_process	transmembrane transport

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P55013

Chain	Residue	Details
A	THR54
B	THR81
A	THR58
A	THR63
A	THR68
A	THR81
B	THR54
B	THR58
B	THR63
B	THR68

site_id	SWS_FT_FI2
Number of Residues	56
Details	TRANSMEM: 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

Chain	Residue	Details
A	VAL229-ILE257
B	VAL229-ILE257

site_id	SWS_FT_FI3
Number of Residues	198
Details	TOPO_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

Chain	Residue	Details
A	ASN258
B	VAL397-PHE453
B	GLU524-LEU525
B	THR585
A	PHE341-PHE348
A	ILE306-THR339
A	VAL397-PHE453
A	GLU524-LEU525
A	THR585
B	ASN258
B	PHE341-PHE348
B	ILE306-THR339

site_id	SWS_FT_FI4
Number of Residues	538
Details	TRANSMEM: 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

Chain	Residue	Details
A	ASP259-LYS284
A	ASN566-LEU584
A	TRP586-LYS606
B	ASP259-LYS284
B	THR304-PHE340
B	PRO349-ALA368
B	MET279-LEU305
B	PHE340-ILE360
B	PRO367-CYS396
B	ALA454-GLU485
B	VAL506-ALA523
A	THR304-PHE340
B	ASN526-ASN554
B	ASN566-LEU584
B	TRP586-LYS606
A	PRO349-ALA368
A	MET279-LEU305
A	PHE340-ILE360
A	PRO367-CYS396
A	ALA454-GLU485
A	VAL506-ALA523
A	ASN526-ASN554

site_id	SWS_FT_FI5
Number of Residues	934
Details	TOPO_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

Chain	Residue	Details
A	ALA285-GLY303
B	ASP486-PRO505
B	SER555-TYR565
B	LYS607-GLN1021
A	GLY278
A	SER361-ASP366
A	ASP486-PRO505
A	SER555-TYR565
A	LYS607-GLN1021
B	ALA285-GLY303
B	GLY278
B	SER361-ASP366

site_id	SWS_FT_FI6
Number of Residues	10
Details	BINDING: 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

Chain	Residue	Details
A	ALA239
B	SER468
A	VAL242
A	ALA464
A	SER467
A	SER468
B	ALA239
B	VAL242
B	ALA464
B	SER467

site_id	SWS_FT_FI7
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ, ECO:0007744\|PDB:8FHR

Chain	Residue	Details
A	ALA240
B	ALA240

site_id	SWS_FT_FI8
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHO, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHQ

Chain	Residue	Details
A	PHE318
B	PHE318

site_id	SWS_FT_FI9
Number of Residues	2
Details	BINDING: 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

Chain	Residue	Details
A	PHE325
B	PHE325

site_id	SWS_FT_FI10
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHP, ECO:0007744\|PDB:8FHR

Chain	Residue	Details
A	THR352
B	THR352

site_id	SWS_FT_FI11
Number of Residues	8
Details	BINDING: BINDING => ECO:0000305\|PubMed:36351028, ECO:0000305\|PubMed:36792826

Chain	Residue	Details
A	GLY353
A	ILE354
A	LEU355
A	TYR540
B	GLY353
B	ILE354
B	LEU355
B	TYR540

site_id	SWS_FT_FI12
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN

Chain	Residue	Details
A	ASN359
B	ASN359

site_id	SWS_FT_FI13
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:36792826, ECO:0007744\|PDB:8FHN, ECO:0007744\|PDB:8FHO

Chain	Residue	Details
A	LEU648
B	GLY741
B	LEU780
B	ASN781
A	ARG655
A	VAL677
A	GLY741
A	LEU780
A	ASN781
B	LEU648
B	ARG655
B	VAL677

site_id	SWS_FT_FI14
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P59158

Chain	Residue	Details
A	VAL134
A	LYS140
A	ALA164
A	GLY217
B	VAL134
B	LYS140
B	ALA164
B	GLY217

site_id	SWS_FT_FI15
Number of Residues	6
Details	MOD_RES: Phosphothreonine; by OXSR1 and STK39 => ECO:0000269\|PubMed:18270262

Chain	Residue	Details
A	GLY137
A	CYS146
A	TRP151
B	GLY137
B	CYS146
B	TRP151

site_id	SWS_FT_FI16
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P59158

Chain	Residue	Details
A	GLY141
A	LEU215
B	GLY141
B	LEU215

site_id	SWS_FT_FI17
Number of Residues	2
Details	MOD_RES: Phosphoserine; by OXSR1 and STK39 => ECO:0000305\|PubMed:18270262, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	THR182
B	THR182

site_id	SWS_FT_FI18
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:36351028, ECO:0007744\|PDB:7Y6I

Chain	Residue	Details
A	ASN406
A	ASN426
B	ASN406
B	ASN426

222415

PDB entries from 2024-07-10

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