Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6X9H

Molecular mechanism and structural basis of small-molecule modulation of acid-sensing ion channel 1 (ASIC1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005272molecular_functionsodium channel activity
A0006814biological_processsodium ion transport
A0015280molecular_functionligand-gated sodium channel activity
A0016020cellular_componentmembrane
B0005272molecular_functionsodium channel activity
B0006814biological_processsodium ion transport
B0015280molecular_functionligand-gated sodium channel activity
B0016020cellular_componentmembrane
C0005272molecular_functionsodium channel activity
C0006814biological_processsodium ion transport
C0015280molecular_functionligand-gated sodium channel activity
C0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS01206
Number of Residues21
DetailsASC Amiloride-sensitive sodium channels signature. YsiTaCridCeTryLVenCnC
ChainResidueDetails
ATYR304-CYS324

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:24507937, ECO:0007744|PDB:4NTW
ChainResidueDetails
ACYS50-LEU71
BCYS50-LEU71
CCYS50-LEU71

site_idSWS_FT_FI2
Number of Residues1056
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:24507937, ECO:0007744|PDB:4NTW
ChainResidueDetails
ATYR72-ALA424
BTYR72-ALA424
CTYR72-ALA424

site_idSWS_FT_FI3
Number of Residues87
DetailsTRANSMEM: Discontinuously helical => ECO:0000305|PubMed:24507937, ECO:0007744|PDB:4NTW
ChainResidueDetails
ATYR425-ASP454
BTYR425-ASP454
CTYR425-ASP454

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Involved in channel desensitization; the process by which the channel becomes unresponsive to proton stimulation => ECO:0000269|PubMed:22842900
ChainResidueDetails
AGLU80
BGLU80
CGLU80

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Involved in proton-dependent gating => ECO:0000250|UniProtKB:P78348
ChainResidueDetails
AASP356
BASP356
CASP356

site_idSWS_FT_FI6
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900, ECO:0007744|PDB:2QTS
ChainResidueDetails
AASN367
AASN394
BASN367
BASN394
CASN367
CASN394

237423

PDB entries from 2025-06-11

PDB statisticsPDBj update infoContact PDBjnumon