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8CQC

Cryo-EM structure of pentameric proteorhodopsin A18L mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0010461molecular_functionlight-activated monoatomic ion channel activity
A0016020cellular_componentmembrane
B0005216molecular_functionmonoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0010461molecular_functionlight-activated monoatomic ion channel activity
B0016020cellular_componentmembrane
C0005216molecular_functionmonoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0010461molecular_functionlight-activated monoatomic ion channel activity
C0016020cellular_componentmembrane
D0005216molecular_functionmonoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0010461molecular_functionlight-activated monoatomic ion channel activity
D0016020cellular_componentmembrane
E0005216molecular_functionmonoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0010461molecular_functionlight-activated monoatomic ion channel activity
E0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYiDWlLTVPLLI
ChainResidueDetails
AARG95-ILE107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues930
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsSite: {"description":"Primary proton acceptor","evidences":[{"source":"PIRSR","id":"PIRSR038142-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsSite: {"description":"Responsible for spectral tuning","evidences":[{"source":"PIRSR","id":"PIRSR038142-1","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsSite: {"description":"Primary proton donor","evidences":[{"source":"PIRSR","id":"PIRSR038142-1","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues5
DetailsSite: {"description":"Proton release group","evidences":[{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues5
DetailsModified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"source":"PubMed","id":"34226545","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7B03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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