6FUF
Crystal structure of the rhodopsin-mini-Go complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0000226 | biological_process | microtubule cytoskeleton organization |
A | 0001750 | cellular_component | photoreceptor outer segment |
A | 0001917 | cellular_component | photoreceptor inner segment |
A | 0001965 | molecular_function | G-protein alpha-subunit binding |
A | 0002046 | molecular_function | opsin binding |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0005085 | molecular_function | guanyl-nucleotide exchange factor activity |
A | 0005502 | molecular_function | 11-cis retinal binding |
A | 0005515 | molecular_function | protein binding |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005886 | cellular_component | plasma membrane |
A | 0005911 | cellular_component | cell-cell junction |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007601 | biological_process | visual perception |
A | 0007602 | biological_process | phototransduction |
A | 0007603 | biological_process | phototransduction, visible light |
A | 0008020 | molecular_function | G protein-coupled photoreceptor activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009416 | biological_process | response to light stimulus |
A | 0009583 | biological_process | detection of light stimulus |
A | 0009642 | biological_process | response to light intensity |
A | 0009881 | molecular_function | photoreceptor activity |
A | 0010467 | biological_process | gene expression |
A | 0016020 | cellular_component | membrane |
A | 0016038 | biological_process | absorption of visible light |
A | 0016056 | biological_process | G protein-coupled opsin signaling pathway |
A | 0019867 | cellular_component | outer membrane |
A | 0042622 | cellular_component | photoreceptor outer segment membrane |
A | 0042802 | molecular_function | identical protein binding |
A | 0042995 | cellular_component | cell projection |
A | 0043052 | biological_process | thermotaxis |
A | 0045494 | biological_process | photoreceptor cell maintenance |
A | 0046872 | molecular_function | metal ion binding |
A | 0050953 | biological_process | sensory perception of light stimulus |
A | 0050960 | biological_process | detection of temperature stimulus involved in thermoception |
A | 0060041 | biological_process | retina development in camera-type eye |
A | 0060342 | cellular_component | photoreceptor inner segment membrane |
A | 0071482 | biological_process | cellular response to light stimulus |
A | 0071800 | biological_process | podosome assembly |
A | 0097225 | cellular_component | sperm midpiece |
A | 0097381 | cellular_component | photoreceptor disc membrane |
A | 0097648 | cellular_component | G protein-coupled receptor complex |
A | 0120200 | cellular_component | rod photoreceptor outer segment |
A | 1904389 | biological_process | rod bipolar cell differentiation |
A | 1990763 | molecular_function | arrestin family protein binding |
A | 1990913 | cellular_component | sperm head plasma membrane |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
B | 0007188 | biological_process | adenylate cyclase-modulating G protein-coupled receptor signaling pathway |
B | 0019001 | molecular_function | guanyl nucleotide binding |
B | 0031683 | molecular_function | G-protein beta/gamma-subunit complex binding |
Functional Information from PROSITE/UniProt
site_id | PS00237 |
Number of Residues | 17 |
Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV |
Chain | Residue | Details |
A | ILE123-VAL139 |
site_id | PS00238 |
Number of Residues | 17 |
Details | OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKTSAvyNPviY |
Chain | Residue | Details |
A | ILE290-TYR306 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | GLY40 | |
B | SER47 | |
B | ASP299 | |
B | GLN305 | |
B | THR324 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250 |
Chain | Residue | Details |
B | ALA302 | |
A | GLU134-HIS152 | |
A | GLN225-ARG252 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: 5-glutamyl histamine => ECO:0000250|UniProtKB:P18872 |
Chain | Residue | Details |
B | ASP328 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250 |
Chain | Residue | Details |
A | THR97-CYS110 | |
A | GLY174-SER202 | |
A | ILE275-ILE286 |
site_id | SWS_FT_FI5 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239 |
Chain | Residue | Details |
A | ASN111-ILE133 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239 |
Chain | Residue | Details |
A | ALA153-VAL173 |
site_id | SWS_FT_FI7 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239 |
Chain | Residue | Details |
A | PHE203-GLY224 |
site_id | SWS_FT_FI8 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239 |
Chain | Residue | Details |
A | MET253-TYR274 |
site_id | SWS_FT_FI9 |
Number of Residues | 21 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17060607, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:17825322, ECO:0000269|PubMed:18563085, ECO:0000269|PubMed:18645239, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:21389983, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23579341, ECO:0000269|PubMed:25205354, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:27458239 |
Chain | Residue | Details |
A | PHE287-MET308 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1HZX |
Chain | Residue | Details |
A | GLU201 | |
A | GLN279 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | SITE: Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:21389983, ECO:0000305|PubMed:22198838, ECO:0000305|PubMed:23579341, ECO:0000305|PubMed:27458239 |
Chain | Residue | Details |
A | GLU113 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-(retinylidene)lysine => ECO:0000269|PubMed:10926528, ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:11972040, ECO:0000269|PubMed:12044163, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16586416, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:17449675, ECO:0000269|PubMed:22198838, ECO:0000269|PubMed:23303210, ECO:0000269|PubMed:27458239, ECO:0000269|PubMed:6870827, ECO:0000305|PubMed:6759163, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1JFP, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO, ECO:0007744|PDB:5DYS |
Chain | Residue | Details |
A | LYS296 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11425302, ECO:0000269|PubMed:15327956, ECO:0000269|PubMed:15491621, ECO:0000269|PubMed:16908857, ECO:0000269|PubMed:18818650, ECO:0000269|PubMed:26526852, ECO:0000269|PubMed:468821, ECO:0000269|PubMed:6759163, ECO:0007744|PDB:1F88, ECO:0007744|PDB:1GZM, ECO:0007744|PDB:1HZX, ECO:0007744|PDB:1U19, ECO:0007744|PDB:2G87, ECO:0007744|PDB:2HPY, ECO:0007744|PDB:2I35, ECO:0007744|PDB:2I36, ECO:0007744|PDB:2I37, ECO:0007744|PDB:2PED, ECO:0007744|PDB:3C9L, ECO:0007744|PDB:3CAP, ECO:0007744|PDB:3DQB, ECO:0007744|PDB:3OAX, ECO:0007744|PDB:3PQR, ECO:0007744|PDB:3PXO, ECO:0007744|PDB:4X1H |
Chain | Residue | Details |
A | CYS2 |
Chain | Residue | Details |
A | ASN15 |