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Yorodumi- PDB-1qh4: CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 A... -
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-Basic information
Entry | Database: PDB / ID: 1qh4 | ||||||
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Title | CRYSTAL STRUCTURE OF CHICKEN BRAIN-TYPE CREATINE KINASE AT 1.41 ANGSTROM RESOLUTION | ||||||
Components | CREATINE KINASE | ||||||
Keywords | TRANSFERASE / BRAIN-TYPE CREATINE KINASE / CANCER / CELLULAR ENERGY METABOLISM / GUANIDINO KINASE / NEURODEGENERATIVE DISORDERS | ||||||
Function / homology | Function and homology information Creatine metabolism / extracellular membrane-bounded organelle / creatine kinase / phosphocreatine biosynthetic process / creatine kinase activity / ATP biosynthetic process / kinase activity / ubiquitin protein ligase binding / extracellular space / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.41 Å | ||||||
Authors | Eder, M. / Schlattner, U. / Becker, A. / Wallimann, T. / Kabsch, W. / Fritz-Wolf, K. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Crystal structure of brain-type creatine kinase at 1.41 A resolution. Authors: Eder, M. / Schlattner, U. / Becker, A. / Wallimann, T. / Kabsch, W. / Fritz-Wolf, K. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1998 Title: Transition State Structure of Arginine Kinase: Implications for Catalysis of Bimolecular Reactions Authors: Zhou, G. / Somasundaram, T. / Blanc, E. / Parthasarathy, G. / Ellington, W.R. / Chapman, M.S. #2: Journal: Nature / Year: 1996 Title: Structure of Mitochondrial Creatine Kinase. Authors: Fritz-Wolf, K. / Schnyder, T. / Wallimann, T. / Kabsch, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qh4.cif.gz | 668.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qh4.ent.gz | 551.4 KB | Display | PDB format |
PDBx/mmJSON format | 1qh4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qh/1qh4 ftp://data.pdbj.org/pub/pdb/validation_reports/qh/1qh4 | HTTPS FTP |
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-Related structure data
Related structure data | 1crkS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 42799.523 Da / Num. of mol.: 4 / Fragment: B CHAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Cellular location: CYTOPLASM / Gene: EMBL-NR. X03509 / Organ: BRAIN / Plasmid: PRF23 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)PLYSS / References: UniProt: P05122, creatine kinase #2: Chemical | ChemComp-ACT / #3: Chemical | ChemComp-CA / | #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: 2.37 Å3/Da / Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: 0.1M MES, 0.4M CA(OAC)2, 15% PE 2MM DTT, PH 6.5, 8 MG/ML PROTEIN | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 48 % | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||
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: EMBL/DESY, HAMBURG / Beamline: BW7B / Wavelength: 0.84 |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jul 22, 1998 / Details: BENT CRYSTAL |
Radiation | Monochromator: GE SINGLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.84 Å / Relative weight: 1 |
Reflection | Resolution: 1.41→38 Å / Num. obs: 301191 / % possible obs: 99.1 % / Redundancy: 4 % / Rmerge(I) obs: 0.042 / Net I/σ(I): 17.2 |
Reflection shell | Resolution: 1.41→1.5 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.215 / Mean I/σ(I) obs: 5 / % possible all: 97.1 |
Reflection shell | *PLUS % possible obs: 97.1 % / Num. unique obs: 49959 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1CRK, MITOCHONDRIAL CREATINE KINASE Resolution: 1.41→6 Å / Num. parameters: 12204 / Num. restraintsaints: 14868 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: X-PLOR AND CNS WERE USED FOR INITIAL REFINEMENT. ANISOTROPIC REFINEMENT IN SHELX REDUCED FREE R (NO CUTOFF) BY 2.6% DISORDERED RESIDUES 321 - 330 (CHAIN A-D) WERE MODELED
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 15 / Occupancy sum hydrogen: 11644 / Occupancy sum non hydrogen: 13358 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.41→6 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 6 Å / σ(F): 0 / % reflection Rfree: 5.3 % / Rfactor obs: 0.134 / Rfactor Rwork: 0.1338 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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