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- PDB-2ycw: TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND B... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ycw | ||||||
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Title | TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL | ||||||
![]() | BETA-1 ADRENERGIC RECEPTOR | ||||||
![]() | RECEPTOR / GPCR / TRANSDUCER / ANTAGONIST BOUND FORM / INTEGRAL MEMBRANE PROTEIN / G-PROTEIN COUPLED RECEPTOR / THERMOSTABILISING POINT MUTATIONS / SEVEN-HELIX RECEPTOR / 7TM RECEPTOR | ||||||
Function / homology | ![]() beta1-adrenergic receptor activity / positive regulation of heart rate by epinephrine-norepinephrine / regulation of circadian sleep/wake cycle, sleep / norepinephrine-epinephrine-mediated vasodilation involved in regulation of systemic arterial blood pressure / adenylate cyclase-activating adrenergic receptor signaling pathway / early endosome / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Moukhametzianov, R. / Warne, T. / Edwards, P.C. / Serrano-Vega, M.J. / Leslie, A.G.W. / Tate, C.G. / Schertler, G.F.X. | ||||||
![]() | ![]() Title: Two Distinct Conformations of Helix 6 Observed in Antagonist-Bound Structures of a Beta-1- Adrenergic Receptor. Authors: Moukhametzianov, R. / Warne, T. / Edwards, P.C. / Serrano-Vega, M.J. / Leslie, A.G. / Tate, C.G. / Schertler, G.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.3 KB | Display | ![]() |
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PDB format | ![]() | 105.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2ycxC ![]() 2ycyC ![]() 2yczC ![]() 2vt4S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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Components
#1: Protein | Mass: 35752.598 Da / Num. of mol.: 2 / Fragment: RESIDUES 33-243,272-276,279-367 / Mutation: YES Source method: isolated from a genetically manipulated source Details: RESIDUES 3-32 AT THE N-TERMINUS AND RESIDUES 244-271 AND 277-278 OF THE THIRD INTRACELLULAR LOOP WERE DELETED FROM THE CONSTRUCT. THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE 367 AND A HEXAHIS TAG ADDED. Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-2CV / #4: Chemical | Compound details | ENGINEERED RESIDUE IN CHAIN A, ARG 68 TO SER ENGINEERED RESIDUE IN CHAIN A, MET 90 TO VAL ...ENGINEERED | Sequence details | THE FOLLOWING MUTATIONS WERE MADE TO IMPROVE THERMOSTABILITY R68S,M90V,Y227A,A282L,F327A,F338M THE ...THE FOLLOWING MUTATIONS WERE MADE TO IMPROVE THERMOSTAB | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.58 Å3/Da / Density % sol: 65.67 % Description: DATA WERE COLLECTED IN WEDGES, SCANNING THE MULTIPLE SPOTS ON THE CRYSTAL |
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Crystal grow | pH: 8.1 / Details: pH 8.1 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 1, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→44.7 Å / Num. obs: 17906 / % possible obs: 86 % / Observed criterion σ(I): 1.5 / Redundancy: 2.4 % / Biso Wilson estimate: 74.7 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 3→3.08 Å / Redundancy: 2 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 1.6 / % possible all: 64 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2VT4 Resolution: 3→44.68 Å / Cor.coef. Fo:Fc: 0.91 / Cor.coef. Fo:Fc free: 0.86 / SU B: 19.335 / SU ML: 0.363 / Cross valid method: THROUGHOUT / ESU R Free: 0.483 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.126 Å2
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Refinement step | Cycle: LAST / Resolution: 3→44.68 Å
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Refine LS restraints |
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