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3WQJ

Crystal structure of archaerhodopsin-2 at 1.8 angstrom resolution

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
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATRP91
ATRP194
AASP217
ALYS221
ATHR95
AMET123
ATRP143
ASER146
ATHR147
ATRP187
ATYR190
APRO191

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 22B A 302
ChainResidue
APHE29
AGLY35
AARG44
AALA48
AILE51
ATHR112
ATHR115
AVAL119
APHE145
ATYR156
ASER160

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
APHE66
AGLY67
AILE68
ASER133
ALYS134
ATHR135
AALA138
AHOH409
AHOH428

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE L2P A 304
ChainResidue
AALA59
AALA63
ATYR85
AALA89
ALEU92
AVAL125
ALEU128
ASQL308
ASQL308

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE L3P A 305
ChainResidue
AILE26

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE L4P A 306
ChainResidue
AILE113

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE L4P A 307
ChainResidue
AGLU45
AALA48
AILE49
AARG110

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SQL A 308
ChainResidue
AL2P304
AL2P304

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 Residues39
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=Helix C","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=Helix D","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=Helix E","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=Helix F","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Pyrrolidone carboxylic acid","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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