+Open data
-Basic information
Entry | Database: PDB / ID: 1isg | |||||||||
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Title | Crystal Structure Analysis of BST-1/CD157 with ATPgammaS | |||||||||
Components | bone marrow stromal cell antigen 1 | |||||||||
Keywords | HYDROLASE / ADP ribosylcyclase / NAD glycohydrolase / cns / ATPgammaS | |||||||||
Function / homology | Function and homology information regulation of cellular extravasation / regulation of superoxide metabolic process / regulation of neutrophil chemotaxis / regulation of integrin-mediated signaling pathway / phosphorus-oxygen lyase activity / Post-translational modification: synthesis of GPI-anchored proteins / uropod / Nicotinate metabolism / regulation of cell-matrix adhesion / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase ...regulation of cellular extravasation / regulation of superoxide metabolic process / regulation of neutrophil chemotaxis / regulation of integrin-mediated signaling pathway / phosphorus-oxygen lyase activity / Post-translational modification: synthesis of GPI-anchored proteins / uropod / Nicotinate metabolism / regulation of cell-matrix adhesion / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / NAD+ nucleosidase activity / NAD+ nucleotidase, cyclic ADP-ribose generating / humoral immune response / specific granule membrane / side of membrane / regulation of peptidyl-tyrosine phosphorylation / positive regulation of B cell proliferation / regulation of calcium-mediated signaling / regulation of actin cytoskeleton organization / regulation of inflammatory response / transferase activity / positive regulation of cell population proliferation / Neutrophil degranulation / signal transduction / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | |||||||||
Authors | Yamamoto-Katayama, S. / Ariyoshi, M. / Ishihara, K. / Hirano, T. / Jingami, H. / Morikawa, K. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities. Authors: Yamamoto-Katayama, S. / Ariyoshi, M. / Ishihara, K. / Hirano, T. / Jingami, H. / Morikawa, K. #1: Journal: Biochem.J. / Year: 2001 Title: Site-directed removal of N-glycosylation sites in BST-1/CD157: effects on molecular and functional heterogeneity Authors: Yamamoto-Katayama, S. / Sato, A. / Ariyoshi, M. / Suyama, M. / Ishihara, K. / Hirano, T. / Nakamura, H. / Morikawa, K. / Jingami, H. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1isg.cif.gz | 117.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1isg.ent.gz | 90.5 KB | Display | PDB format |
PDBx/mmJSON format | 1isg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1isg_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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Full document | 1isg_full_validation.pdf.gz | 1.6 MB | Display | |
Data in XML | 1isg_validation.xml.gz | 22.9 KB | Display | |
Data in CIF | 1isg_validation.cif.gz | 30.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/is/1isg ftp://data.pdbj.org/pub/pdb/validation_reports/is/1isg | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 30172.182 Da / Num. of mol.: 2 / Fragment: Extracellular region / Mutation: N34D, N63T, N116A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q10588, NAD+ glycohydrolase #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | #4: Water | ChemComp-HOH / | |
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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: 3.57 Å3/Da / Density % sol: 65.57 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: ammonium sulfate, citrate, ATPgammaS, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: unknown | |||||||||||||||||||||||||
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: SPring-8 / Beamline: BL24XU / Wavelength: 0.836 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Mar 18, 2000 |
Radiation | Monochromator: silicon crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.836 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→20 Å / Num. all: 26538 / Num. obs: 26538 / % possible obs: 98.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 31.2 % / Biso Wilson estimate: 26.9 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 5.9 |
Reflection shell | Resolution: 2.6→2.69 Å / Rmerge(I) obs: 0.371 / Mean I/σ(I) obs: 33.6 / Num. unique all: 2504 / % possible all: 94.2 |
Reflection | *PLUS Lowest resolution: 20 Å |
Reflection shell | *PLUS % possible obs: 94.2 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→19.4 Å / Rfactor Rfree error: 0.006 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 34.5738 Å2 / ksol: 0.361196 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.6→19.4 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.6→2.76 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 20 Å / σ(F): 0 / % reflection Rfree: 7.5 % / Rfactor obs: 0.211 / Rfactor Rfree: 0.25 | ||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 45.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.337 / % reflection Rfree: 7.2 % / Rfactor Rwork: 0.292 |