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- PDB-2ckq: Crystal structure of Human Choline Kinase alpha 2 in complex with... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ckq | ||||||
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Title | Crystal structure of Human Choline Kinase alpha 2 in complex with Phosphocholine | ||||||
![]() | CHOLINE KINASE ALPHA | ||||||
![]() | TRANSFERASE / PHOSPHATIDYLCHOLINE / PHOSPHOLIPID SYNTHESIS | ||||||
Function / homology | ![]() ethanolamine kinase / choline kinase / ethanolamine kinase activity / CDP-choline pathway / choline kinase activity / Synthesis of PE / phosphatidylethanolamine biosynthetic process / lipid droplet disassembly / phosphatidylcholine biosynthetic process / cholinesterase activity ...ethanolamine kinase / choline kinase / ethanolamine kinase activity / CDP-choline pathway / choline kinase activity / Synthesis of PE / phosphatidylethanolamine biosynthetic process / lipid droplet disassembly / phosphatidylcholine biosynthetic process / cholinesterase activity / lipid transport / Synthesis of PC / cellular response to glucose starvation / lipid droplet / lipid metabolic process / protein tyrosine kinase activity / phosphorylation / protein homodimerization activity / ATP binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Malito, E. / Lavie, A. | ||||||
![]() | ![]() Title: Elucidation of Human Choline Kinase Crystal Structures in Complex with the Products Adp or Phosphocholine. Authors: Malito, E. / Sekulic, N. / Too, W.C. / Konrad, M. / Lavie, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 153.7 KB | Display | ![]() |
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PDB format | ![]() | 118.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.9 KB | Display | ![]() |
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Full document | ![]() | 460.8 KB | Display | |
Data in XML | ![]() | 27.1 KB | Display | |
Data in CIF | ![]() | 37.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ckoC ![]() 2ckpC ![]() 1nw1S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 45376.262 Da / Num. of mol.: 2 / Fragment: SPLICE ISOFORM 2, RESIDUES 50-439 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P35790, choline kinase, ethanolamine kinase #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE DESCRIBES THE HUMAN CHOLINE KINASE ISOFORM ALFA-2, ACCORDING TO AYOAMA ET AL., 2000. ...THE SEQUENCE DESCRIBES THE HUMAN CHOLINE KINASE ISOFORM ALFA-2, ACCORDING TO AYOAMA ET AL., 2000. THE SEQUENCE FROM OUR CONSTRUCT LACKS THE FIRST N-TERMINAL 49 RESIDUES. THE SEQUENCE BELOW CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.64 Å3/Da / Density % sol: 65.9 % |
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Crystal grow | pH: 7.5 / Details: 0.01 M MGCL2, 15% PEG 3350, 0.2 M NAF., pH 7.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 12, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. obs: 46369 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 8.1 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 13.9 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 6.1 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 3.2 / % possible all: 99.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1NW1 Resolution: 2.4→15 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.909 / SU B: 17.554 / SU ML: 0.198 / TLS residual ADP flag: UNVERIFIED / Cross valid method: THROUGHOUT / ESU R: 0.294 / ESU R Free: 0.238 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.66 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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Refine LS restraints |
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