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Yorodumi- PDB-4qnq: Crystal Structure Analysis of full-length Bcl-XL in complex with ... -
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-Basic information
Entry | Database: PDB / ID: 4qnq | ||||||
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Title | Crystal Structure Analysis of full-length Bcl-XL in complex with the inhibitor ABT-263 | ||||||
Components | Bcl-2-like protein 1 | ||||||
Keywords | APOPTOSIS/APOPTOSIS inhibitor / ALPHA-HELICAL PROTEIN / APOPTOSIS / APOPTOSIS-APOPTOSIS inhibitor complex | ||||||
Function / homology | Function and homology information response to erythropoietin / cellular response to astaxanthin / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members / The NLRP1 inflammasome / cellular response to erythropoietin / synaptic vesicle recycling via endosome / positive regulation of synaptic vesicle exocytosis / positive regulation of synaptic vesicle clustering / RAS processing / cellular response to prolactin ...response to erythropoietin / cellular response to astaxanthin / BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members / The NLRP1 inflammasome / cellular response to erythropoietin / synaptic vesicle recycling via endosome / positive regulation of synaptic vesicle exocytosis / positive regulation of synaptic vesicle clustering / RAS processing / cellular response to prolactin / BH domain binding / apoptotic process in bone marrow cell / dendritic cell apoptotic process / dendritic cell proliferation / positive regulation of synaptic vesicle endocytosis / positive regulation of mononuclear cell proliferation / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / negative regulation of dendritic cell apoptotic process / negative regulation of execution phase of apoptosis / negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / fertilization / negative regulation of protein localization to plasma membrane / regulation of mitochondrial membrane permeability / regulation of growth / Bcl-2 family protein complex / regulation of long-term synaptic depression / response to cycloheximide / clathrin binding / positive regulation of ATP biosynthetic process / cellular response to alkaloid / hepatocyte apoptotic process / negative regulation of reproductive process / negative regulation of developmental process / negative regulation of release of cytochrome c from mitochondria / BH3 domain binding / germ cell development / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / response to inorganic substance / cellular response to nitric oxide / ectopic germ cell programmed cell death / MDM2/MDM4 family protein binding / cellular response to interleukin-1 / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / negative regulation of intrinsic apoptotic signaling pathway / response to electrical stimulus / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / cellular response to cAMP / ovarian follicle development / extrinsic apoptotic signaling pathway in absence of ligand / response to organonitrogen compound / response to endoplasmic reticulum stress / mitochondrion organization / cellular response to dexamethasone stimulus / release of cytochrome c from mitochondria / regulation of cytokinesis / regulation of mitochondrial membrane potential / epithelial cell proliferation / response to cytokine / response to ischemia / mitochondrial membrane / cellular response to amino acid stimulus / response to lead ion / response to virus / cellular response to gamma radiation / response to radiation / response to hydrogen peroxide / response to organic cyclic compound / cerebral cortex development / synaptic vesicle membrane / response to peptide hormone / endocytosis / male gonad development / intrinsic apoptotic signaling pathway in response to DNA damage / cellular response to xenobiotic stimulus / presynapse / GTPase binding / cellular response to tumor necrosis factor / cellular response to hypoxia / spermatogenesis / nuclear membrane / neuron apoptotic process / regulation of apoptotic process / in utero embryonic development / response to oxidative stress / mitochondrial outer membrane / negative regulation of neuron apoptotic process / response to lipopolysaccharide / mitochondrial inner membrane / response to hypoxia / mitochondrial matrix / response to xenobiotic stimulus / positive regulation of apoptotic process / protein heterodimerization activity / centrosome / apoptotic process / protein-containing complex binding / negative regulation of apoptotic process / protein kinase binding / endoplasmic reticulum / protein homodimerization activity Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Korste, A. / Vetter, I.R. / Stoll, R. | ||||||
Citation | Journal: TO BE PUBLISHED Title: Crystal Structure Analysis of full-length Bcl-XL in complex with the inhibitor ABT-263 Authors: Korste, A. / Vetter, I.R. / Stoll, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4qnq.cif.gz | 382.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4qnq.ent.gz | 312.8 KB | Display | PDB format |
PDBx/mmJSON format | 4qnq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qn/4qnq ftp://data.pdbj.org/pub/pdb/validation_reports/qn/4qnq | HTTPS FTP |
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-Related structure data
Related structure data | 1r2dS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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12 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: GLY / End label comp-ID: GLY / Refine code: 4 / Auth seq-ID: 2 - 196 / Label seq-ID: 9 - 203
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-Components
#1: Protein | Mass: 26854.664 Da / Num. of mol.: 12 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: B2CL1_RAT, Bcl2l1, Bclx, Blc2l / Plasmid: pTXB1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P53563 #2: Chemical | ChemComp-1XJ / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.66 Å3/Da / Density % sol: 25.69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 20% (w/v) PEG 3350, 0.2 M Calcium Chloride, pH approx. 7.8, vapor diffusion, hanging drop, temperature 293K PH range: approx. 7.8 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.06997 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: PILATUS 6M / Detector: PIXEL / Date: Nov 10, 2012 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.06997 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.3→47.036 Å / Num. obs: 89549 / % possible obs: 97.4 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.104 / Net I/σ(I): 6.89 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1r2d Resolution: 2.3→85 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.937 / Occupancy max: 1 / Occupancy min: 1 / SU B: 9.207 / SU ML: 0.213 / Cross valid method: THROUGHOUT / ESU R: 0.373 / ESU R Free: 0.25 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.066 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→85 Å
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Refine LS restraints |
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