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7B03

Cryo-EM structure of the green-light absorbing proteorhodopsin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0007602biological_processphototransduction
A0009881molecular_functionphotoreceptor activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0007602biological_processphototransduction
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0007602biological_processphototransduction
C0009881molecular_functionphotoreceptor activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0007602biological_processphototransduction
D0009881molecular_functionphotoreceptor activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0005216molecular_functionmonoatomic ion channel activity
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0007602biological_processphototransduction
E0009881molecular_functionphotoreceptor activity
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
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

239803

PDB entries from 2025-08-06

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