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7RTU

Cryo-EM structure of a TTYH2 trans-dimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0005225molecular_functionvolume-sensitive anion channel activity
A0005229molecular_functionintracellularly calcium-gated chloride channel activity
A0005254molecular_functionchloride channel activity
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0015813biological_processL-glutamate transmembrane transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0072320molecular_functionvolume-sensitive chloride channel activity
A1902476biological_processchloride transmembrane transport
B0005225molecular_functionvolume-sensitive anion channel activity
B0005229molecular_functionintracellularly calcium-gated chloride channel activity
B0005254molecular_functionchloride channel activity
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0015813biological_processL-glutamate transmembrane transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034707cellular_componentchloride channel complex
B0072320molecular_functionvolume-sensitive chloride channel activity
B1902476biological_processchloride transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues454
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsMotif: {"description":"RGD","evidences":[{"source":"PubMed","id":"34824283","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34824283","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RTT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Essential for the formation of the channel-pore","evidences":[{"source":"PubMed","id":"31138989","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9BSA4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"34824283","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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