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Yorodumi- PDB-2luv: Structure and Binding Interface of the Cytosolic Tails of aXb2 In... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2luv | ||||||
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Title | Structure and Binding Interface of the Cytosolic Tails of aXb2 Integrin | ||||||
Components | Integrin alpha-X | ||||||
Keywords | CELL ADHESION / MYRISTOYLATED / DPC MICELLES | ||||||
Function / homology | Function and homology information positive regulation of endothelial tube morphogenesis / integrin alphaX-beta2 complex / positive regulation of myelination / heterotypic cell-cell adhesion / integrin complex / cell adhesion mediated by integrin / tertiary granule membrane / ficolin-1-rich granule membrane / ECM proteoglycans / Integrin cell surface interactions ...positive regulation of endothelial tube morphogenesis / integrin alphaX-beta2 complex / positive regulation of myelination / heterotypic cell-cell adhesion / integrin complex / cell adhesion mediated by integrin / tertiary granule membrane / ficolin-1-rich granule membrane / ECM proteoglycans / Integrin cell surface interactions / cell-matrix adhesion / secretory granule membrane / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / animal organ morphogenesis / cell-cell adhesion / receptor tyrosine kinase binding / positive regulation of angiogenesis / integrin binding / signaling receptor activity / Interleukin-4 and Interleukin-13 signaling / defense response to virus / cell adhesion / positive regulation of cell migration / external side of plasma membrane / positive regulation of cell population proliferation / Neutrophil degranulation / positive regulation of gene expression / cell surface / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Chua, G.L. / Tang, X. / Patra, T.A. / Tan, S.M. / Bhattacharjya, S. | ||||||
Citation | Journal: To be Published Title: Structure and Binding Interface of the Cytosolic Tails of aXb2 Integrin Authors: Chua, G.L. / Tang, X. / Patra, T.A. / Tan, S.M. / Bhattacharjya, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2luv.cif.gz | 247.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2luv.ent.gz | 211 KB | Display | PDB format |
PDBx/mmJSON format | 2luv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lu/2luv ftp://data.pdbj.org/pub/pdb/validation_reports/lu/2luv | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3960.423 Da / Num. of mol.: 1 / Fragment: Cytoplasmic domain, UNP residues 1129-1163 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P20702 |
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Sequence details | THIS PEPTIDE IS CHEMICALLY |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0 / pH: 5.6 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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NMR constraints | NOE constraints total: 263 / NOE intraresidue total count: 74 / NOE long range total count: 3 / NOE medium range total count: 96 / NOE sequential total count: 90 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 29 / Protein psi angle constraints total count: 28 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Average torsion angle constraint violation: 8.9 ° / Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0 Å / Maximum torsion angle constraint violation: 8.9 ° / Maximum upper distance constraint violation: 0 Å / Representative conformer: 1 | ||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0 Å / Distance rms dev error: 0 Å |