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Open data
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Basic information
| Entry | Database: PDB / ID: 1jlm | ||||||
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| Title | I-DOMAIN FROM INTEGRIN CR3, MN2+ BOUND | ||||||
Components | INTEGRIN | ||||||
Keywords | CELL ADHESION PROTEIN / INTEGRIN / GLYCOPROTEIN | ||||||
| Function / homology | Function and homology informationectodermal cell differentiation / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / response to Gram-positive bacterium / response to curcumin / positive regulation of microglial cell mediated cytotoxicity / vertebrate eye-specific patterning / : / complement component C3b binding / complement-mediated synapse pruning ...ectodermal cell differentiation / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / response to Gram-positive bacterium / response to curcumin / positive regulation of microglial cell mediated cytotoxicity / vertebrate eye-specific patterning / : / complement component C3b binding / complement-mediated synapse pruning / Toll Like Receptor 4 (TLR4) Cascade / complement receptor mediated signaling pathway / cargo receptor activity / integrin complex / heterotypic cell-cell adhesion / phagocytosis, engulfment / cell adhesion mediated by integrin / negative regulation of dopamine metabolic process / forebrain development / amyloid-beta clearance / tertiary granule membrane / plasma membrane raft / positive regulation of protein targeting to membrane / Integrin cell surface interactions / response to mechanical stimulus / specific granule membrane / positive regulation of superoxide anion generation / heat shock protein binding / receptor-mediated endocytosis / response to ischemia / cell-matrix adhesion / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / microglial cell activation / cell-cell adhesion / integrin binding / response to estradiol / amyloid-beta binding / Interleukin-4 and Interleukin-13 signaling / cell adhesion / innate immune response / external side of plasma membrane / Neutrophil degranulation / cell surface / extracellular space / extracellular exosome / metal ion binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Lee, J.-O. / Liddington, R. | ||||||
Citation | Journal: Structure / Year: 1995Title: Two conformations of the integrin A-domain (I-domain): a pathway for activation? Authors: Lee, J.O. / Bankston, L.A. / Arnaout, M.A. / Liddington, R.C. #1: Journal: Cell(Cambridge,Mass.) / Year: 1995Title: Crystal Structure of the a Domain from the Alpha Subunit of Integrin Cr3 (Cd11B/Cd18) Authors: Lee, J.O. / Rieu, P. / Arnaout, M.A. / Liddington, R. #2: Journal: Cell(Cambridge,Mass.) / Year: 1993Title: A Novel Divalent Cation-Binding Site in the a Domain of the Beta 2 Integrin Cr3 (Cd11B/Cd18) is Essential for Ligand Binding Authors: Michishita, M. / Videm, V. / Arnaout, M.A. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1jlm.cif.gz | 52.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1jlm.ent.gz | 36.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1jlm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1jlm_validation.pdf.gz | 418.3 KB | Display | wwPDB validaton report |
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| Full document | 1jlm_full_validation.pdf.gz | 421.2 KB | Display | |
| Data in XML | 1jlm_validation.xml.gz | 10.4 KB | Display | |
| Data in CIF | 1jlm_validation.cif.gz | 14 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jl/1jlm ftp://data.pdbj.org/pub/pdb/validation_reports/jl/1jlm | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1idoS 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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| Unit cell |
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Components
| #1: Protein | Mass: 21994.117 Da / Num. of mol.: 1 / Fragment: I-DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX-2T / Production host: ![]() |
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| #2: Chemical | ChemComp-MN / |
| #3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.19 Å3/Da / Density % sol: 43.8 % | ||||||||||||||||||||||||||||||||||||
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| Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C / Wavelength: 0.98 |
| Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
| Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
| Reflection | Resolution: 2→12 Å / Num. obs: 12933 / % possible obs: 99.5 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.06 |
| Reflection shell | Resolution: 2→2.07 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.269 / % possible all: 98.5 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1IDO Resolution: 2→12 Å / σ(F): 2
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| Displacement parameters | Biso mean: 26 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2→12 Å
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| Refine LS restraints |
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| Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS
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Homo sapiens (human)
X-RAY DIFFRACTION
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