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2M6I

Putative pentameric open-channel structure of full-length transmembrane domains of human glycine receptor alpha1 subunit

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues105
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues50
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23994010","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues5
DetailsSite: {"description":"Important for obstruction of the ion pore in the closed conformation","evidences":[{"source":"PubMed","id":"25730860","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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