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2L6X

Solution NMR Structure of Proteorhodopsin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0007602biological_processphototransduction
A0009881molecular_functionphotoreceptor activity
A0010461molecular_functionlight-activated monoatomic ion channel activity
A0016020cellular_componentmembrane
A1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATRP98
ALYS231
AVAL133
APHE137
AALA151
AILE154
ATRP197
ATYR200
AASP227
AASN230

Functional Information from PROSITE/UniProt
site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYiDWlLTVPLLI
ChainResidueDetails
AARG94-ILE106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues143
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLY30-VAL49
ALEU62-ILE84
ALEU99-GLY121
ALEU128-ALA147
AALA151-ALA168
AMET189-GLY211
ALEU221-VAL243

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Primary proton acceptor
ChainResidueDetails
AASP97

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Responsible for spectral tuning
ChainResidueDetails
ALEU105

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Primary proton donor
ChainResidueDetails
AGLU108

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000250
ChainResidueDetails
ALYS231

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PDB entries from 2024-07-31

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