[English] 日本語
![](img/lk-miru.gif)
- PDB-4bwb: Structure of Evolved Agonist-bound Neurotensin Receptor 1 Mutant ... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4bwb | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of Evolved Agonist-bound Neurotensin Receptor 1 Mutant without Lysozyme Fusion | ||||||
![]() |
| ||||||
![]() | SIGNALING PROTEIN / G PROTEIN COUPLED RECEPTOR / MEMBRANE PROTEIN | ||||||
Function / homology | ![]() response to antipsychotic drug / Peptide ligand-binding receptors / neuropeptide receptor binding / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / symmetric synapse / response to mineralocorticoid / D-aspartate import across plasma membrane / positive regulation of gamma-aminobutyric acid secretion / regulation of membrane depolarization ...response to antipsychotic drug / Peptide ligand-binding receptors / neuropeptide receptor binding / G protein-coupled neurotensin receptor activity / inositol phosphate catabolic process / symmetric synapse / response to mineralocorticoid / D-aspartate import across plasma membrane / positive regulation of gamma-aminobutyric acid secretion / regulation of membrane depolarization / L-glutamate import across plasma membrane / positive regulation of arachidonic acid secretion / regulation of respiratory gaseous exchange / neuron spine / positive regulation of inhibitory postsynaptic potential / neuropeptide hormone activity / hyperosmotic response / digestive tract development / negative regulation of systemic arterial blood pressure / negative regulation of release of sequestered calcium ion into cytosol / positive regulation of glutamate secretion / G alpha (q) signalling events / positive regulation of inositol phosphate biosynthetic process / temperature homeostasis / response to corticosterone / response to lipid / cellular response to lithium ion / detection of temperature stimulus involved in sensory perception of pain / response to axon injury / neuropeptide signaling pathway / axon terminus / transport vesicle / response to amphetamine / blood vessel diameter maintenance / adult locomotory behavior / cellular response to dexamethasone stimulus / positive regulation of release of sequestered calcium ion into cytosol / cellular response to nerve growth factor stimulus / liver development / response to cocaine / dendritic shaft / learning / visual learning / terminal bouton / cytoplasmic side of plasma membrane / response to estradiol / perikaryon / dendritic spine / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor ligand activity / positive regulation of apoptotic process / membrane raft / axon / negative regulation of gene expression / neuronal cell body / dendrite / protein-containing complex binding / positive regulation of gene expression / negative regulation of apoptotic process / cell surface / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Egloff, P. / Hillenbrand, M. / Scott, D.J. / Schlinkmann, K.M. / Heine, P. / Balada, S. / Batyuk, A. / Mittl, P. / Plueckthun, A. | ||||||
![]() | ![]() Title: Structure of Signaling-Competent Neurotensin Receptor 1 Obtained by Directed Evolution in Escherichia Coli Authors: Egloff, P. / Hillenbrand, M. / Klenk, C. / Batyuk, A. / Heine, P. / Balada, S. / Schlinkmann, K.M. / Scott, D.J. / Schuetz, M. / Plueckthun, A. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 133.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 104.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 462.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 468.8 KB | Display | |
Data in XML | ![]() | 22.2 KB | Display | |
Data in CIF | ![]() | 29.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3zevC ![]() 4buoSC ![]() 4bv0C C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.4579, 0.1531, -0.875), Vector: |
-
Components
#1: Protein | Mass: 37598.082 Da / Num. of mol.: 2 / Fragment: RESIDUES 50-390 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1087.277 Da / Num. of mol.: 2 / Fragment: C-TERMINUS, RESIDUES 157-162 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Sequence details | CHAIN A, B HAS MUTATION AT FOLLOWING POSITIONS S83G,A86L, ...CHAIN A, B HAS MUTATION AT FOLLOWING POSITIONS S83G,A86L, S101R,H103D,H105Y,L119F,M121L,E124D,R143K,D150E,A161V, R167L,R213L,V234L,K235R,V240L,I253A,I260A,N262R, K263R,H305R,C332V,F342A,T354S,F358V,S362A.FURTHERMOR | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.88 Å3/Da / Density % sol: 68.34 % / Description: NONE |
---|---|
Crystal grow | pH: 5.5 Details: 20% (V/V) PEG600, 0.2 M CACL2, 50 MM NAACETATE PH 5.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.56→50 Å / Num. obs: 14522 / % possible obs: 99.7 % / Redundancy: 7.2 % / Biso Wilson estimate: 174.88 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 8.88 |
Reflection shell | Resolution: 3.56→3.7 Å / Redundancy: 7.6 % / Mean I/σ(I) obs: 0.32 / % possible all: 98.4 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4BUO Resolution: 3.57→21.88 Å / SU ML: 0.76 / σ(F): 1.35 / Phase error: 51.92 / Stereochemistry target values: ML / Details: PHENIX AND REFMAC WERE USED
| ||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.57→21.88 Å
| ||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|