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6L6N

hASIC1a co-crystallized with Nafamostat

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
ATYR305-CYS325

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsTRANSMEM: Helical => ECO:0000305|PubMed:34319232, ECO:0007744|PDB:7RNN
ChainResidueDetails
APHE50-GLN66
BPHE50-GLN66
CPHE50-GLN66

site_idSWS_FT_FI2
Number of Residues1080
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:34319232, ECO:0007744|PDB:7RNN
ChainResidueDetails
ATYR67-GLU427
BTYR67-GLU427
CTYR67-GLU427

site_idSWS_FT_FI3
Number of Residues90
DetailsTRANSMEM: Discontinuously helical => ECO:0000305|PubMed:34319232, ECO:0007744|PDB:7RNN
ChainResidueDetails
AILE428-TYR458
BILE428-TYR458
CILE428-TYR458

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Involved in channel desensitization; the process by which the channel becomes unresponsive to proton stimulation => ECO:0000250|UniProtKB:Q1XA76
ChainResidueDetails
AGLU79
BGLU79
CGLU79

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Involved in the inhibition by the spider venom psalmotoxin-1 => ECO:0000269|PubMed:19654327
ChainResidueDetails
APHE352
BPHE352
CPHE352

site_idSWS_FT_FI6
Number of Residues3
DetailsSITE: Involved in proton-dependent gating => ECO:0000269|PubMed:19654327
ChainResidueDetails
AASP357
BASP357
CASP357

site_idSWS_FT_FI7
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:32915133, ECO:0000269|PubMed:34319232, ECO:0007744|PDB:7CFS, ECO:0007744|PDB:7CFT, ECO:0007744|PDB:7RNN
ChainResidueDetails
AASN368
AASN395
BASN368
BASN395
CASN368
CASN395

237735

PDB entries from 2025-06-18

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