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Yorodumi- PDB-1fjm: Protein serine/threonine phosphatase-1 (alpha isoform, type 1) co... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fjm | |||||||||
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Title | Protein serine/threonine phosphatase-1 (alpha isoform, type 1) complexed with microcystin-LR toxin | |||||||||
Components |
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Keywords | HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE / TOXIN / HYDROLASE-HYDROLASE INHIBITOR complex | |||||||||
Function / homology | Function and homology information fatty acid derivative binding / regulation of translational initiation by eIF2 alpha dephosphorylation / protein serine/threonine phosphatase activity => GO:0004722 / protein serine/threonine phosphatase activity => GO:0004722 / protein phosphatase type 1 complex / regulation of glycogen catabolic process / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / peptidyl-serine dephosphorylation ...fatty acid derivative binding / regulation of translational initiation by eIF2 alpha dephosphorylation / protein serine/threonine phosphatase activity => GO:0004722 / protein serine/threonine phosphatase activity => GO:0004722 / protein phosphatase type 1 complex / regulation of glycogen catabolic process / PTW/PP1 phosphatase complex / glycogen granule / regulation of glycogen biosynthetic process / peptidyl-serine dephosphorylation / beta-catenin destruction complex disassembly / peptidyl-threonine dephosphorylation / protein phosphatase 1 binding / cadherin binding involved in cell-cell adhesion / positive regulation of extrinsic apoptotic signaling pathway in absence of ligand / regulation of canonical Wnt signaling pathway / myosin phosphatase activity / protein serine/threonine phosphatase activity / branching morphogenesis of an epithelial tube / glycogen metabolic process / protein-serine/threonine phosphatase / entrainment of circadian clock by photoperiod / Triglyceride catabolism / phosphatase activity / protein phosphatase activator activity / phosphoprotein phosphatase activity / DARPP-32 events / ribonucleoprotein complex binding / dephosphorylation / viral process / Downregulation of TGF-beta receptor signaling / protein dephosphorylation / negative regulation of protein binding / adherens junction / lung development / response to lead ion / circadian regulation of gene expression / regulation of circadian rhythm / positive regulation of canonical Wnt signaling pathway / Circadian Clock / presynapse / perikaryon / dendritic spine / cell cycle / cell division / glutamatergic synapse / nucleolus / extracellular exosome / nucleoplasm / metal ion binding / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Oryctolagus cuniculus (rabbit) Microcystis aeruginosa (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | |||||||||
Authors | Goldberg, J. / Nairn, A.C. / Kuriyan, J. | |||||||||
Citation | Journal: Nature / Year: 1995 Title: Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Authors: Goldberg, J. / Huang, H.B. / Kwon, Y.G. / Greengard, P. / Nairn, A.C. / Kuriyan, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fjm.cif.gz | 137.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fjm.ent.gz | 106.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fjm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fj/1fjm ftp://data.pdbj.org/pub/pdb/validation_reports/fj/1fjm | 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.251034, -0.966528, 0.052974), Vector: |
-Components
#1: Protein | Mass: 37558.051 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) References: UniProt: P08129, UniProt: P62139*PLUS, protein-serine/threonine phosphatase #2: Protein/peptide | #3: Chemical | ChemComp-MN / #4: Chemical | #5: Water | ChemComp-HOH / | Compound details | ELECTRON DENSITY MAPS SHOW THAT RESIDUE CYSTEINE 127 IS OXIDIZED, WITH A TERMINAL SULPHINYL OR ...ELECTRON DENSITY MAPS SHOW THAT RESIDUE CYSTEINE 127 IS OXIDIZED, WITH A TERMINAL SULPHINYL OR SULPHONYL GROUP. HOWEVER, THE TERMINAL OXYGEN ATOMS OF THE SIDE CHAIN HAVE NOT BEEN MODELLED. | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.86 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / 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 | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 20 Å / Num. obs: 38768 / % possible obs: 99.5 % / Num. measured all: 180676 / Rmerge(I) obs: 0.056 |
Reflection shell | *PLUS % possible obs: 97.2 % / Rmerge(I) obs: 0.136 |
-Processing
Software |
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Refinement | Resolution: 2.1→6 Å / Rfactor Rwork: 0.178 / Rfactor obs: 0.178 / σ(F): 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→6 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection all: 36974 / Rfactor all: 0.178 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |