1H2S
Molecular basis of transmenbrane signalling by sensory rhodopsin II-transducer complex
- PDB DOI: https://doi.org/10.2210/pdb1H2S/pdb
- Classification: MEMBRANE PROTEIN
- Organism(s): Natronomonas pharaonis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No 
- Membrane Protein: Yes  OPMPDBTMMemProtMDmpstruc
- Deposited: 2002-08-15 Released: 2002-10-10 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.93 Å
- R-Value Free: 0.258 
- R-Value Work: 0.226 
- R-Value Observed: 0.226 
This is version 1.6 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
SENSORY RHODOPSIN II | 225 | Natronomonas pharaonis | Mutation(s): 0  Membrane Entity: Yes  | ||
UniProt | |||||
Find proteins for P42196 (Natronomonas pharaonis) Explore P42196  Go to UniProtKB:  P42196 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P42196 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
SENSORY RHODOPSIN II TRANSDUCER | 60 | Natronomonas pharaonis | Mutation(s): 0  Membrane Entity: Yes  | ||
UniProt | |||||
Find proteins for P42259 (Natronomonas pharaonis) Explore P42259  Go to UniProtKB:  P42259 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P42259 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
Ligands 2 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
BOG Query on BOG | C [auth A] | octyl beta-D-glucopyranoside C14 H28 O6 HEGSGKPQLMEBJL-RKQHYHRCSA-N | |||
RET Query on RET | D [auth A] | RETINAL C20 H28 O NCYCYZXNIZJOKI-OVSJKPMPSA-N |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.93 Å
- R-Value Free: 0.258 
- R-Value Work: 0.226 
- R-Value Observed: 0.226 
- Space Group: P 21 21 2
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 124.3 | α = 90 |
b = 46.96 | β = 90 |
c = 53.84 | γ = 90 |
Software Name | Purpose |
---|---|
CNS | refinement |
MOSFLM | data reduction |
SCALA | data scaling |
MOLREP | phasing |
Entry History 
Deposition Data
- Released Date: 2002-10-10  Deposition Author(s): Gordeliy, V.I., Labahn, J., Moukhametzianov, R., Efremov, R., Granzin, J., Schlesinger, R., Bueldt, G., Savopol, T., Scheidig, A., Klare, J.P., Engelhard, M.
Revision History (Full details and data files)
- Version 1.0: 2002-10-10
Type: Initial release - Version 1.1: 2011-05-08
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2019-05-08
Changes: Advisory, Data collection, Derived calculations, Experimental preparation, Other - Version 1.4: 2019-05-22
Changes: Advisory, Data collection, Derived calculations, Experimental preparation - Version 1.5: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Derived calculations, Other, Structure summary - Version 1.6: 2023-12-13
Changes: Advisory, Data collection, Database references, Refinement description, Structure summary