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- PDB-1bbz: CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bbz | ||||||
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Title | CRYSTAL STRUCTURE OF THE ABL-SH3 DOMAIN COMPLEXED WITH A DESIGNED HIGH-AFFINITY PEPTIDE LIGAND: IMPLICATIONS FOR SH3-LIGAND INTERACTIONS | ||||||
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![]() | COMPLEX (TRANSFERASE/PEPTIDE) / COMPLEX (TRANSFERASE-PEPTIDE) / ![]() ![]() | ||||||
Function / homology | ![]() : / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / protein localization to cytoplasmic microtubule plus-end / DNA conformation change / podocyte apoptotic process / DN4 thymocyte differentiation / Role of ABL in ROBO-SLIT signaling / response to epinephrine / transitional one stage B cell differentiation ...: / positive regulation of actin filament binding / positive regulation of oxidoreductase activity / protein localization to cytoplasmic microtubule plus-end / DNA conformation change / podocyte apoptotic process / DN4 thymocyte differentiation / Role of ABL in ROBO-SLIT signaling / response to epinephrine / transitional one stage B cell differentiation / activation of protein kinase C activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Pisabarro, M.T. / Serrano, L. / Wilmanns, M. | ||||||
![]() | ![]() Title: Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions. Authors: Pisabarro, M.T. / Serrano, L. / Wilmanns, M. #1: ![]() Title: Rational Design of Specific High-Affinity Peptide Ligands for the Abl-SH3 Domain Authors: Pisabarro, M.T. / Serrano, L. #2: ![]() Title: High-Resolution Crystal Structures of Tyrosine Kinase SH3 Domains Complexed with Proline-Rich Peptides Authors: Musacchio, A. / Saraste, M. / Wilmanns, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 69.3 KB | Display | ![]() |
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PDB format | ![]() | 54.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1aboS 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 6423.080 Da / Num. of mol.: 4 / Fragment: SH3 DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1035.149 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source #3: Chemical | ChemComp-SO4 / ![]() #4: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.68 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Method: vapor diffusion / pH: 3.1 Details: CRYSTALS WITH DIMENSIONS 0.25X0.25X0.25 MM3 WERE OBTAINED AT ROOM TEMPERATURE BY VAPOUR DIFFUSION AGAINST A RESERVOIR CONTAINING 0.1 M CITRIC ACID PH 3.1, 2 M AMMONIUM SULPHATE, 0.2 M SODIUM ...Details: CRYSTALS WITH DIMENSIONS 0.25X0.25X0.25 MM3 WERE OBTAINED AT ROOM TEMPERATURE BY VAPOUR DIFFUSION AGAINST A RESERVOIR CONTAINING 0.1 M CITRIC ACID PH 3.1, 2 M AMMONIUM SULPHATE, 0.2 M SODIUM CHLORIDE, AND 1MM DTT/EDTA. THE HANGING DROP CONTAINED 1:1 RATIO OF RESERVOIR AND PROTEIN-PEPTIDE SOLUTIONS., vapor diffusion | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.6→39.3 Å / Num. obs: 226846 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6.59 % / Biso Wilson estimate: 15.4 Å2 / Rmerge(I) obs: 0.058 / Rsym value: 0.058 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 1.6→1.63 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 1.9 / Rsym value: 0.58 / % possible all: 98.4 |
Reflection | *PLUS Num. obs: 34430 / Num. measured all: 226846 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1ABO Resolution: 1.65→8 Å / Cross valid method: FREE R-FACTOR / σ(F): 1
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Displacement parameters | Biso mean: 13.5 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→8 Å
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Refine LS restraints |
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Xplor file |
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