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4L35

Crystal structure of cruxrhodopsin-3 at pH5 from Haloarcula vallismortis at 2.1 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 Residues14
DetailsBINDING SITE FOR RESIDUE RET A 301
ChainResidue
ATYR81
ATRP186
ATYR189
APRO190
ATRP193
ALYS220
ATRP84
ATHR87
ATHR88
ALEU91
AMET116
ATRP142
ASER145
ATHR146

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 22B A 302
ChainResidue
AGLY29
ATRP30
ATYR41
APHE52
AASN104
ATHR105
ALEU112
APHE148
ASER159

Functional Information from PROSITE/UniProt
site_idPS00327
Number of Residues12
DetailsBACTERIAL_OPSIN_RET Bacterial rhodopsins retinal binding site. FMVIDLvAKvGF
ChainResidueDetails
APHE212-PHE223

site_idPS00950
Number of Residues13
DetailsBACTERIAL_OPSIN_1 Bacterial rhodopsins signature 1. RYsDWlFTTPLLL
ChainResidueDetails
AARG80-LEU92

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues47
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:25268964
ChainResidueDetails
AMET1-ILE9
AGLY61-TYR77
ASER126-ARG138
AGLY196-ILE207

site_idSWS_FT_FI2
Number of Residues17
DetailsTRANSMEM: Helical; Name=Helix A => ECO:0000269|PubMed:25268964
ChainResidueDetails
ATRP10-ALA27

site_idSWS_FT_FI3
Number of Residues62
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25268964
ChainResidueDetails
AARG28-TYR41
ALEU95-THR105
ASER159-LYS176
ALEU228-ASP250

site_idSWS_FT_FI4
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix B => ECO:0000269|PubMed:25268964
ChainResidueDetails
AILE42-LEU60

site_idSWS_FT_FI5
Number of Residues16
DetailsTRANSMEM: Helical; Name=Helix C => ECO:0000269|PubMed:25268964
ChainResidueDetails
ATRP78-ASP94

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix D => ECO:0000269|PubMed:25268964
ChainResidueDetails
AILE106-LEU125

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix E => ECO:0000269|PubMed:25268964
ChainResidueDetails
ALEU139-SER158

site_idSWS_FT_FI8
Number of Residues18
DetailsTRANSMEM: Helical; Name=Helix F => ECO:0000269|PubMed:25268964
ChainResidueDetails
ATHR177-VAL195

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=Helix G => ECO:0000269|PubMed:25268964
ChainResidueDetails
AGLU208-LEU227

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Primary proton acceptor => ECO:0000250|UniProtKB:P02945
ChainResidueDetails
AASP83

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:25268964, ECO:0007744|PDB:4JR8, ECO:0007744|PDB:4L35
ChainResidueDetails
ALYS220

237735

PDB entries from 2025-06-18

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