+Open data
-Basic information
Entry | Database: PDB / ID: 1lfa | ||||||
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Title | CD11A I-DOMAIN WITH BOUND MN++ | ||||||
Components | CD11AIntegrin alpha L | ||||||
Keywords | CELL ADHESION | ||||||
Function / homology | Function and homology information memory T cell extravasation / integrin alphaL-beta2 complex / T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell / ICAM-3 receptor activity / RUNX3 Regulates Immune Response and Cell Migration / integrin complex / cell adhesion mediated by integrin / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / leukocyte cell-cell adhesion / receptor clustering ...memory T cell extravasation / integrin alphaL-beta2 complex / T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell / ICAM-3 receptor activity / RUNX3 Regulates Immune Response and Cell Migration / integrin complex / cell adhesion mediated by integrin / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / leukocyte cell-cell adhesion / receptor clustering / Integrin cell surface interactions / specific granule membrane / phagocytosis / cell adhesion molecule binding / cell-matrix adhesion / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / cell-cell adhesion / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / integrin binding / cell adhesion / inflammatory response / external side of plasma membrane / Neutrophil degranulation / cell surface / signal transduction / extracellular exosome / membrane / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.8 Å | ||||||
Authors | Leahy, D.J. / Qu, A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1995 Title: Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin. Authors: Qu, A. / Leahy, D.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lfa.cif.gz | 115.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lfa.ent.gz | 89.7 KB | Display | PDB format |
PDBx/mmJSON format | 1lfa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lf/1lfa ftp://data.pdbj.org/pub/pdb/validation_reports/lf/1lfa | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 281 / 2: CIS PROLINE - PRO B 281 |
-Components
#1: Protein | Mass: 21323.494 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: REFOLDED FROM UREA / Plasmid: PET11C / Production host: Escherichia coli (E. coli) / References: UniProt: P20701 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45.96 % Description: MAD DATA AT 4 DIFFERENT WAVE LENGTHS WAS COLLECTED AT THE NSLS IN FEB-95 ON A CRYSTAL IN SPACE GROUP P 2 2 2 OF SELENOMETHIONYL-SUBSTITUTED PROTEIN. AN INITIAL STRUCTURE WAS DETERMINED ...Description: MAD DATA AT 4 DIFFERENT WAVE LENGTHS WAS COLLECTED AT THE NSLS IN FEB-95 ON A CRYSTAL IN SPACE GROUP P 2 2 2 OF SELENOMETHIONYL-SUBSTITUTED PROTEIN. AN INITIAL STRUCTURE WAS DETERMINED FROM THIS MAD DATA AND USED AS A MOLECULAR REPLACEMENT SEARCH MODEL FOR THE DATA COLLECTED ON A NATIVE CRYSTAL IN SPACE GROUP C 2. | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.2 / Details: pH 5.2 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Wavelength: 1.5418 Å |
Detector | Date: Sep 1, 1994 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→30 Å / Num. obs: 27543 / % possible obs: 76 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Rmerge(I) obs: 0.04 |
-Processing
Software |
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Refinement | Resolution: 1.8→6 Å / σ(F): 2
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Displacement parameters | Biso mean: 14.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor all: 0.193 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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