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2Z55

Bacterioruberin in the trimeric structure of archaerhodopsin-2

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
A1902600biological_processproton transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0007602biological_processphototransduction
B0009881molecular_functionphotoreceptor activity
B0016020cellular_componentmembrane
B1902600biological_processproton transmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0007602biological_processphototransduction
D0009881molecular_functionphotoreceptor activity
D0016020cellular_componentmembrane
D1902600biological_processproton transmembrane transport
E0005216molecular_functionmonoatomic ion channel activity
E0005886cellular_componentplasma membrane
E0006811biological_processmonoatomic ion transport
E0007602biological_processphototransduction
E0009881molecular_functionphotoreceptor activity
E0016020cellular_componentmembrane
E1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVtAKvGF
ChainResidueDetails
APHE213-PHE224

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
AARG87-LEU99

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues145
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=Helix C","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues88
DetailsTransmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues112
DetailsTransmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues112
DetailsTransmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues128
DetailsTransmembrane: {"description":"Helical; Name=Helix G","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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