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Yorodumi- PDB-1jsg: CRYSTAL STRUCTURE OF P14TCL1, AN ONCOGENE PRODUCT INVOLVED IN T-C... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jsg | ||||||
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Title | CRYSTAL STRUCTURE OF P14TCL1, AN ONCOGENE PRODUCT INVOLVED IN T-CELL PROLYMPHOCYTIC LEUKEMIA, REVEALS A NOVEL B-BARREL TOPOLOGY | ||||||
Components | ONCOGENE PRODUCT P14TCL1 | ||||||
Keywords | PROTO-ONCOGENE / CL1 GENE / T CELL LEUKEMIA / ONCOPROTEIN / MICROSOME | ||||||
Function / homology | Function and homology information multicellular organism development / positive regulation of mitochondrial membrane potential / protein serine/threonine kinase activator activity / positive regulation of protein-containing complex assembly / positive regulation of protein serine/threonine kinase activity / positive regulation of peptidyl-serine phosphorylation / cellular response to tumor necrosis factor / positive regulation of cell population proliferation / negative regulation of apoptotic process / protein kinase binding ...multicellular organism development / positive regulation of mitochondrial membrane potential / protein serine/threonine kinase activator activity / positive regulation of protein-containing complex assembly / positive regulation of protein serine/threonine kinase activity / positive regulation of peptidyl-serine phosphorylation / cellular response to tumor necrosis factor / positive regulation of cell population proliferation / negative regulation of apoptotic process / protein kinase binding / endoplasmic reticulum / protein-containing complex / nucleoplasm / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Hoh, F. / Yang, Y.-S. / Guignard, L. / Padilla, A. / Stern, R.-H. / Lhoste, J.-M. / Van Tilbeurgh, H. | ||||||
Citation | Journal: Structure / Year: 1998 Title: Crystal structure of p14TCL1, an oncogene product involved in T-cell prolymphocytic leukemia, reveals a novel beta-barrel topology. Authors: Hoh, F. / Yang, Y.S. / Guignard, L. / Padilla, A. / Stern, M.H. / Lhoste, J.M. / van Tilbeurgh, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jsg.cif.gz | 34.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jsg.ent.gz | 23.9 KB | Display | PDB format |
PDBx/mmJSON format | 1jsg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/js/1jsg ftp://data.pdbj.org/pub/pdb/validation_reports/js/1jsg | 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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Details | P14 IS INVOLVED IN RARE FORMS OF LEUKEMIA BUT ITS CELLULAR ROLE REMAINS UNKNOWN. THERE EXISTS EVIDENCE FOR DIMER FORMATION IN SOLUTION BUT THE PROTEIN IS PRESENT AS A MONOMER IN THE ASYMMETRIC UNIT. A TIGHT DIMER CONTACT IS GENERATED BY THE TWO-FOLD CRYSTAL C-AXIS. |
-Components
#1: Protein | Mass: 13475.537 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell: T-CELL / References: UniProt: P56279 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.52 Å3/Da / Density % sol: 65.02 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Biso Wilson estimate: 37 Å2 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 40 Å / Num. obs: 6870 / % possible obs: 99.4 % / Redundancy: 8.8 % / Num. measured all: 60407 / Rmerge(I) obs: 0.099 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.6 Å / % possible obs: 99.9 % / Rmerge(I) obs: 0.288 |
-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / Rfactor Rfree error: 0.01 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 29.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.5→2.65 Å / Rfactor Rfree error: 0.034 / Total num. of bins used: 6
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Xplor file |
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Software | *PLUS Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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