+Open data
-Basic information
Entry | Database: PDB / ID: 1jfp | ||||||
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Title | Structure of bovine rhodopsin (dark adapted) | ||||||
Components | rhodopsin | ||||||
Keywords | SIGNALING PROTEIN / MEMBRANE PROTEIN / G-protein coupled receptor | ||||||
Function / homology | Function and homology information Opsins / VxPx cargo-targeting to cilium / rod photoreceptor outer segment / rod bipolar cell differentiation / sperm head plasma membrane / podosome assembly / absorption of visible light / opsin binding / The canonical retinoid cycle in rods (twilight vision) / : ...Opsins / VxPx cargo-targeting to cilium / rod photoreceptor outer segment / rod bipolar cell differentiation / sperm head plasma membrane / podosome assembly / absorption of visible light / opsin binding / The canonical retinoid cycle in rods (twilight vision) / : / G protein-coupled photoreceptor activity / photoreceptor inner segment membrane / rhodopsin mediated signaling pathway / 11-cis retinal binding / cellular response to light stimulus / G protein-coupled receptor complex / Inactivation, recovery and regulation of the phototransduction cascade / phototransduction, visible light / thermotaxis / Activation of the phototransduction cascade / detection of temperature stimulus involved in thermoception / outer membrane / arrestin family protein binding / photoreceptor cell maintenance / photoreceptor outer segment membrane / G alpha (i) signalling events / response to light stimulus / phototransduction / photoreceptor outer segment / G-protein alpha-subunit binding / sperm midpiece / visual perception / guanyl-nucleotide exchange factor activity / microtubule cytoskeleton organization / photoreceptor disc membrane / cell-cell junction / gene expression / G protein-coupled receptor signaling pathway / Golgi membrane / zinc ion binding / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Yeagle, P.L. / Choi, G. / Albert, A.D. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms. Authors: Yeagle, P.L. / Choi, G. / Albert, A.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jfp.cif.gz | 119.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jfp.ent.gz | 92.3 KB | Display | PDB format |
PDBx/mmJSON format | 1jfp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jf/1jfp ftp://data.pdbj.org/pub/pdb/validation_reports/jf/1jfp | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 39031.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P02699 |
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#2: Chemical | ChemComp-RET / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: fragments of rhodopsin / Solvent system: aqueous or DMSO |
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Sample conditions | Ionic strength: 10 mM / pH: 6 / Pressure: 1 atm / Temperature: 283 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Software ordinal: 1 Details: SECONDARY STRUCTURE FROM NMR STRUCTURES OF PEPTIDES ENCODING HELICES OR TURNS, AND LONG-RANGE DISTANCE CONSTRAINTS FROM OTHER MEASUREMENTS ON INTACT PROTEIN AMINO TERMINUS REMOVED DUE TO ...Details: SECONDARY STRUCTURE FROM NMR STRUCTURES OF PEPTIDES ENCODING HELICES OR TURNS, AND LONG-RANGE DISTANCE CONSTRAINTS FROM OTHER MEASUREMENTS ON INTACT PROTEIN AMINO TERMINUS REMOVED DUE TO LACK OF LONG-RANGE CONSTRAINTS | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 3 / Conformers submitted total number: 1 |