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Yorodumi- PDB-3l2d: Glycocyamine kinase, beta-beta homodimer from marine worm Namalyc... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3l2d | ||||||
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Title | Glycocyamine kinase, beta-beta homodimer from marine worm Namalycastis sp. | ||||||
Components | Glycocyamine kinase beta chain | ||||||
Keywords | TRANSFERASE / phosphagen kinase / glycocyamine kinase / Kinase | ||||||
Function / homology | Function and homology information phosphocreatine biosynthetic process / creatine kinase activity / mitochondrion / ATP binding Similarity search - Function | ||||||
Biological species | Namalycastis sp. ST01 (invertebrata) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Lim, K. / Pullalarevu, S. / Herzberg, O. | ||||||
Citation | Journal: Biochemistry / Year: 2010 Title: Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member. Authors: Lim, K. / Pullalarevu, S. / Surabian, K.T. / Howard, A. / Suzuki, T. / Moult, J. / Herzberg, O. #1: Journal: COMP.BIOCHEM.PHYSIOL. B: BIOCHEM.MOL.BIOL. / Year: 2005 Title: Isolation, characterization, and cDNA-derived amino acid sequence of glycocyamine kinase from the tropical marine worm Namalycastis sp. Authors: Mizuta, C. / Tanaka, K. / Suzuki, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3l2d.cif.gz | 303 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3l2d.ent.gz | 247.7 KB | Display | PDB format |
PDBx/mmJSON format | 3l2d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3l2d_validation.pdf.gz | 453.3 KB | Display | wwPDB validaton report |
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Full document | 3l2d_full_validation.pdf.gz | 484.3 KB | Display | |
Data in XML | 3l2d_validation.xml.gz | 60.1 KB | Display | |
Data in CIF | 3l2d_validation.cif.gz | 84 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l2/3l2d ftp://data.pdbj.org/pub/pdb/validation_reports/l2/3l2d | HTTPS FTP |
-Related structure data
Related structure data | 3l2eC 4v7nC 1qh4S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 44108.363 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Namalycastis sp. ST01 (invertebrata) / Gene: GK-beta, GK_beta / Plasmid: pGK_beta221 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21star(DE3) / References: UniProt: Q6AW42, EC: 2.7.3.1 #2: 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: 2.23 Å3/Da / Density % sol: 44.82 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 22% polyethylene glycol 3350, 0.2M sodium nitrate, 0.1M Tris HCl, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: May 20, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 60423 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.8 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 11.6 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.344 / Mean I/σ(I) obs: 3.5 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1QH4 Resolution: 2.4→50 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 43 Å2 | |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→50 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.49 Å / Rfactor Rfree: 0.341 / Rfactor Rwork: 0.276 |