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6GUZ

Ground state structure of Archaerhodopsin-3 obtained from LCP crystals using a thin-film sandwich at room temperature

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 Residues11
Detailsbinding site for residue RET A 300
ChainResidue
ATRP96
AASP222
ALYS226
ATHR99
ATHR100
ATRP148
ASER151
ATHR152
ATRP192
ATYR195
ATRP199

site_idAC2
Number of Residues4
Detailsbinding site for residue R16 A 302
ChainResidue
ATHR120
AGLY123
AVAL223
ADD9311

site_idAC3
Number of Residues1
Detailsbinding site for residue DD9 A 303
ChainResidue
AD10317

site_idAC4
Number of Residues2
Detailsbinding site for residue R16 A 304
ChainResidue
AILE32
APHE231

site_idAC5
Number of Residues2
Detailsbinding site for residue DD9 A 309
ChainResidue
ALEU28
ALEU68

site_idAC6
Number of Residues1
Detailsbinding site for residue DD9 A 310
ChainResidue
ALEU68

site_idAC7
Number of Residues1
Detailsbinding site for residue DD9 A 311
ChainResidue
AR16302

site_idAC8
Number of Residues1
Detailsbinding site for residue D10 A 317
ChainResidue
ADD9303

site_idAC9
Number of Residues6
Detailsbinding site for residue CA A 713
ChainResidue
AASP11
AASP46
AASP48
ALEU240
AHOH586
AHOH589

site_idAD1
Number of Residues6
Detailsbinding site for residue NA A 714
ChainResidue
AASP11
ALEU12
ALEU13
AASP15
AARG17
ATHR20

site_idAD2
Number of Residues5
Detailsbinding site for residue CL A 715
ChainResidue
AALA8
AGLY210
AGLY212
AILE213
APRO246

site_idAD3
Number of Residues2
Detailsbinding site for residue CL A 716
ChainResidue
ALYS47
AHOH575

site_idAD4
Number of Residues2
Detailsbinding site for residue CL A 717
ChainResidue
ATHR45
AASP46

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVLDVtAKvGF
ChainResidueDetails
APHE218-PHE229

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYaDWlFTTPLLL
ChainResidueDetails
AARG92-LEU104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=Helix A","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=Helix B","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues27
DetailsTopological domain: {"description":"Extracellular","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":"N6-(retinylidene)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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