+Open data
-Basic information
Entry | Database: PDB / ID: 1g86 | ||||||
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Title | CHARCOT-LEYDEN CRYSTAL PROTEIN/N-ETHYLMALEIMIDE COMPLEX | ||||||
Components | CHARCOT-LEYDEN CRYSTAL PROTEIN | ||||||
Keywords | HYDROLASE / beta barrel | ||||||
Function / homology | Function and homology information regulation of activated T cell proliferation / regulation of T cell cytokine production / T cell apoptotic process / regulation of T cell anergy / cysteine-type endopeptidase activity involved in apoptotic process / carbohydrate binding / collagen-containing extracellular matrix / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | Ackerman, S.J. / Liu, L. / Kwatia, M.A. / Savage, M.P. / Leonidas, D.D. / Swaminathan, G.J. / Acharya, K.R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2002 Title: Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. Authors: Ackerman, S.J. / Liu, L. / Kwatia, M.A. / Savage, M.P. / Leonidas, D.D. / Swaminathan, G.J. / Acharya, K.R. #1: Journal: Biochemistry / Year: 1999 Title: Selective Recognition of Mannose by Human Eosinophil Charcot-Leyden Crystal Protein (Galectin-10): a Crystallographic Study at 1.8 A Resolution. Authors: Swaminathan, G.J. / Leonidas, D.D. / Savage, M.P. / Ackerman, S.J. / Acharya, K.R. #2: Journal: Structure / Year: 1995 Title: Crystal Structure of Human Charcot-Leyden Crystal Protein, an Eosinophil Lysophospholipase, Identifies it as a New Member of the Carbohydrate-binding Family of Galectins. Authors: Leonidas, D.D. / Elbert, B.L. / Zhou, Z. / Leffler, H. / Ackerman, S.J. / Acharya, K.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g86.cif.gz | 44.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g86.ent.gz | 31.2 KB | Display | PDB format |
PDBx/mmJSON format | 1g86.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1g86_validation.pdf.gz | 379.3 KB | Display | wwPDB validaton report |
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Full document | 1g86_full_validation.pdf.gz | 381.2 KB | Display | |
Data in XML | 1g86_validation.xml.gz | 4.9 KB | Display | |
Data in CIF | 1g86_validation.cif.gz | 7.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g8/1g86 ftp://data.pdbj.org/pub/pdb/validation_reports/g8/1g86 | HTTPS FTP |
-Related structure data
Related structure data | 1hdkC 1lclS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 16499.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: EOSINOPHIL PRIMARY GRANULE / Source: (natural) Homo sapiens (human) / References: UniProt: Q05315, lysophospholipase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.86 Å3/Da / Density % sol: 57.01 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Tris-Acetate 0.1M, pH7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.8→20 Å / Num. all: 17870 / Num. obs: 17573 / % possible obs: 93.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.08 % / Biso Wilson estimate: 15.5 Å2 / Rmerge(I) obs: 0.132 / Rsym value: 0.053 / Net I/σ(I): 12.8 | ||||||||||||||||||
Reflection shell | Resolution: 1.8→1.91 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.233 / Mean I/σ(I) obs: 7.2 / Num. unique all: 2832 / Rsym value: 0.182 / % possible all: 91.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1LCL Resolution: 1.8→20 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 24.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.029 / Total num. of bins used: 6
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Xplor file |
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