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Yorodumi- PDB-1dkt: CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 COMPLEX WIT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dkt | ||||||
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Title | CKSHS1: HUMAN CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1 COMPLEX WITH METAVANADATE | ||||||
Components | CYCLIN DEPENDENT KINASE SUBUNIT, TYPE 1Cyclin-dependent kinase | ||||||
Keywords | CELL DIVISION | ||||||
Function / homology | Function and homology information mitotic cell cycle phase transition / cyclin-dependent protein serine/threonine kinase activator activity / SCF ubiquitin ligase complex / cyclin-dependent protein kinase holoenzyme complex / regulation of mitotic cell cycle / ubiquitin binding / SCF(Skp2)-mediated degradation of p27/p21 / Cyclin D associated events in G1 / histone binding / fibroblast proliferation ...mitotic cell cycle phase transition / cyclin-dependent protein serine/threonine kinase activator activity / SCF ubiquitin ligase complex / cyclin-dependent protein kinase holoenzyme complex / regulation of mitotic cell cycle / ubiquitin binding / SCF(Skp2)-mediated degradation of p27/p21 / Cyclin D associated events in G1 / histone binding / fibroblast proliferation / cell division / regulation of DNA-templated transcription / protein kinase binding / nucleoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.9 Å | ||||||
Authors | Bourne, Y. / Arvai, A.S. / Tainer, J.A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Crystal structure of the human cell cycle protein CksHs1: single domain fold with similarity to kinase N-lobe domain. Authors: Arvai, A.S. / Bourne, Y. / Hickey, M.J. / Tainer, J.A. #1: Journal: Proteins / Year: 1995 Title: Crystallization and Preliminary Crystallographic Study of Human Ckshs1: A Cell Cycle Regulatory Protein Authors: Arvai, A.S. / Bourne, Y. / Williams, D. / Reed, S.I. / Tainer, J.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dkt.cif.gz | 43.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dkt.ent.gz | 32.1 KB | Display | PDB format |
PDBx/mmJSON format | 1dkt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dk/1dkt ftp://data.pdbj.org/pub/pdb/validation_reports/dk/1dkt | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.18391, -0.95094, -0.248777), Vector: Details | THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 B 5 .. B 75 A 5 .. A 75 0.905 | |
-Components
#1: Protein | Mass: 9679.211 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PBR322 / Production host: Escherichia coli (E. coli) / Strain (production host): BL-ZI / References: UniProt: P61024 #2: Chemical | ChemComp-V7O / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.33 Å3/Da / Density % sol: 71.61 % | ||||||||||||||||||||||||||||||
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Crystal | *PLUS Density % sol: 72 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→40 Å / Num. obs: 7655 / % possible obs: 94 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Rmerge(I) obs: 0.038 / Net I/σ(I): 25 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 2 % / Rmerge(I) obs: 0.15 / Mean I/σ(I) obs: 5 / % possible all: 80 |
Reflection | *PLUS Redundancy: 3 % / Rmerge(I) obs: 0.038 |
Reflection shell | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 3 Å / % possible obs: 80 % / Redundancy: 2 % / Rmerge(I) obs: 0.15 / Mean I/σ(I) obs: 5 |
-Processing
Software |
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Refinement | Resolution: 2.9→6 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.9→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |