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Open data
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Basic information
Entry | Database: PDB / ID: 4cim | ||||||
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Title | Complex of a Bcl-w BH3 mutant with a BH3 domain | ||||||
![]() | (BCL-2-LIKE PROTEIN 2) x 2 | ||||||
![]() | APOPTOSIS / CELL DEATH | ||||||
Function / homology | ![]() negative regulation of mitochondrial membrane permeability / Sertoli cell proliferation / BH domain binding / Bcl-2 family protein complex / negative regulation of release of cytochrome c from mitochondria / cellular response to glycine / negative regulation of intrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / cellular response to estradiol stimulus / response to ischemia ...negative regulation of mitochondrial membrane permeability / Sertoli cell proliferation / BH domain binding / Bcl-2 family protein complex / negative regulation of release of cytochrome c from mitochondria / cellular response to glycine / negative regulation of intrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / cellular response to estradiol stimulus / response to ischemia / cellular response to amyloid-beta / intrinsic apoptotic signaling pathway in response to DNA damage / disordered domain specific binding / spermatogenesis / regulation of apoptotic process / mitochondrial outer membrane / protein heterodimerization activity / protein-containing complex binding / negative regulation of apoptotic process / protein homodimerization activity / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Colman, P.M. / Lee, E.F. / Fairlie, W.D. | ||||||
![]() | ![]() Title: The Functional Differences of Pro-Survival and Pro-Apoptotic B Cell Lymphoma 2 (Bcl-2) Proteins Depend on Structural Differences in Their Bcl-2 Homology 3 (Bh3) Domains Authors: Lee, E.F. / Dewson, G. / Evangelista, M. / Pettikiriarachchi, A. / Zhu, H. / Colman, P.M. / Fairlie, W.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 149.4 KB | Display | ![]() |
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PDB format | ![]() | 118.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471.6 KB | Display | ![]() |
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Full document | ![]() | 475.5 KB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 25.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cinC ![]() 2y6wS C: citing same article ( S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 17801.867 Da / Num. of mol.: 2 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 2336.583 Da / Num. of mol.: 2 / Fragment: RESIDUES 38-58 / Mutation: YES Source method: isolated from a genetically manipulated source Details: PEPTIDE FROM PROTEOLYTIC CLEAVAGE BCL-W DURING PURIFICATION Source: (gene. exp.) ![]() ![]() ![]() #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | Sequence details | MUTATIONS IN SEQUENCE AS FOLLOWS C29S H43G M46L A49I A128E C-TERMINAL TRUNCATION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.7 % / Description: NONE |
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Crystal grow | pH: 8 / Details: 1 M TRISODIUM CITRATE 0.1 M IMIDAZOLE, PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.954 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→50 Å / Num. obs: 51625 / % possible obs: 99.4 % / Observed criterion σ(I): 2 / Redundancy: 3.78 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.93 |
Reflection shell | Resolution: 1.5→1.59 Å / Redundancy: 3.64 % / Rmerge(I) obs: 0.85 / Mean I/σ(I) obs: 1.57 / % possible all: 96.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2Y6W Resolution: 1.5→44.229 Å
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Refinement step | Cycle: LAST / Resolution: 1.5→44.229 Å
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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