+Open data
-Basic information
Entry | Database: PDB / ID: 4xbm | ||||||
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Title | X-ray crystal structure of Notch ligand Delta-like 1 | ||||||
Components | Delta-like protein 1 | ||||||
Keywords | SIGNALING PROTEIN / ectodomain EGF-like repeat Ligand C2 domain | ||||||
Function / homology | Function and homology information cerebellar molecular layer formation / regulation of skeletal muscle tissue growth / Notch signaling pathway involved in arterial endothelial cell fate commitment / skin epidermis development / proximal tubule development / negative regulation of epidermal cell differentiation / regulation of vascular endothelial growth factor signaling pathway / somite specification / lateral inhibition / loop of Henle development ...cerebellar molecular layer formation / regulation of skeletal muscle tissue growth / Notch signaling pathway involved in arterial endothelial cell fate commitment / skin epidermis development / proximal tubule development / negative regulation of epidermal cell differentiation / regulation of vascular endothelial growth factor signaling pathway / somite specification / lateral inhibition / loop of Henle development / skeletal muscle tissue growth / retina morphogenesis in camera-type eye / endothelial tip cell fate specification / MECP2 regulates transcription of neuronal ligands / nephron development / cerebellar Purkinje cell layer structural organization / negative regulation of cardiac muscle cell differentiation / marginal zone B cell differentiation / negative regulation of inner ear auditory receptor cell differentiation / regulation of somitogenesis / positive regulation of skeletal muscle tissue growth / neuron fate specification / compartment pattern specification / Constitutive Signaling by NOTCH1 t(7;9)(NOTCH1:M1580_K2555) Translocation Mutant / negative regulation of myeloid cell differentiation / negative regulation of glial cell apoptotic process / left/right axis specification / proximal/distal pattern formation / type B pancreatic cell development / neuronal stem cell population maintenance / Tat protein binding / astrocyte development / clathrin-dependent endocytosis / cell fate determination / negative regulation of myoblast differentiation / Notch binding / determination of left/right symmetry / regulation of growth / negative regulation of epithelial cell differentiation / organ growth / spinal cord development / negative regulation of interleukin-10 production / positive regulation of endocytosis / positive regulation of Notch signaling pathway / regulation of cell division / heart looping / negative regulation of Notch signaling pathway / positive regulation of sprouting angiogenesis / plasma membrane => GO:0005886 / inner ear development / negative regulation of cell differentiation / hemopoiesis / negative regulation of neuron differentiation / regulation of neurogenesis / somitogenesis / regulation of cell adhesion / energy homeostasis / Notch signaling pathway / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / NOTCH3 Activation and Transmission of Signal to the Nucleus / adherens junction / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / regulation of blood pressure / retina development in camera-type eye / cytoplasmic vesicle / scaffold protein binding / cell differentiation / membrane raft / apical plasma membrane / negative regulation of cell population proliferation / calcium ion binding / positive regulation of cell population proliferation / positive regulation of transcription by RNA polymerase II / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.2 Å | ||||||
Authors | Kershaw, N.J. / Burgess, A.W. / Church, N.L. / Luo, C.S. / Adam, T.E. | ||||||
Funding support | Australia, 1items
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Citation | Journal: Biochem.J. / Year: 2015 Title: Notch ligand delta-like1: X-ray crystal structure and binding affinity. Authors: Kershaw, N.J. / Church, N.L. / Griffin, M.D. / Luo, C.S. / Adams, T.E. / Burgess, A.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4xbm.cif.gz | 146.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4xbm.ent.gz | 109.8 KB | Display | PDB format |
PDBx/mmJSON format | 4xbm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xb/4xbm ftp://data.pdbj.org/pub/pdb/validation_reports/xb/4xbm | HTTPS FTP |
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-Related structure data
Related structure data | 4cbzS S: Starting model for refinement |
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Similar structure data |
-Links
-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: 57430.820 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DLL1, UNQ146/PRO172 / Cell line (production host): 293F / Production host: Homo sapiens (human) / References: UniProt: O00548 #2: Sugar | ChemComp-FUC / | |
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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: 3.77 Å3/Da / Density % sol: 67.39 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.4M potassium thiocyanate 16% PEG3350 0.1M Bis-tris propane pH 7.5 5mM CaCl2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Apr 30, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→67.4 Å / Num. obs: 29271 / % possible obs: 99.9 % / Redundancy: 7.2 % / Rmerge(I) obs: 0.432 / Net I/σ(I): 6.27 |
Reflection shell | Resolution: 3.2→3.314 Å |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4CBZ Resolution: 3.2→67.3 Å / SU ML: 0.55 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 30.47 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→67.3 Å
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Refine LS restraints |
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LS refinement shell |
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