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Yorodumi- PDB-7ruv: Structure of Human ATP:Cobalamin Adenosyltransferase E193K bound ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7ruv | ||||||
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Title | Structure of Human ATP:Cobalamin Adenosyltransferase E193K bound to adenosylcobalamin | ||||||
Components | Corrinoid adenosyltransferase | ||||||
Keywords | TRANSFERASE / ATP:cobalamin adenosyl transferase / cobalamin / vitamin B12 / patient mutation | ||||||
Function / homology | Function and homology information Defective MMAB causes MMA, cblB type / cobalamin metabolic process / Cobalamin (Cbl) metabolism / corrinoid adenosyltransferase activity / Transferases; Transferring alkyl or aryl groups, other than methyl groups / cobalamin binding / transferase activity, transferring alkyl or aryl (other than methyl) groups / mitochondrial matrix / ATP binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Mascarenhas, R. / Gouda, H. / Koutmos, M. / Banerjee, R. | ||||||
Funding support | United States, 1items
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Citation | Journal: J.Biol.Chem. / Year: 2021 Title: Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions. Authors: Gouda, H. / Mascarenhas, R. / Pillay, S. / Ruetz, M. / Koutmos, M. / Banerjee, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7ruv.cif.gz | 145.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7ruv.ent.gz | 111.6 KB | Display | PDB format |
PDBx/mmJSON format | 7ruv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ru/7ruv ftp://data.pdbj.org/pub/pdb/validation_reports/ru/7ruv | HTTPS FTP |
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-Related structure data
Related structure data | 7rutC 7ruuC 2idxS S: Starting model for refinement C: citing same article (ref.) |
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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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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 21720.760 Da / Num. of mol.: 4 / Mutation: E193K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MMAB / Production host: Escherichia coli (E. coli) / References: UniProt: Q96EY8, corrinoid adenosyltransferase |
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-Non-polymers , 6 types, 125 molecules
#2: Chemical | ChemComp-K / | ||||||||
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#3: Chemical | #4: Chemical | ChemComp-B12 / #5: Chemical | ChemComp-5AD / #6: Chemical | ChemComp-GOL / | #7: Water | ChemComp-HOH / | |
-Details
Has ligand of interest | Y |
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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: 2.76 Å3/Da / Density % sol: 55.45 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: 50 mM HEPES pH 7.5, 150 mM KCl, 2 mM MgCl2, 2 mM TCEP and 5% glycerol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-D / Wavelength: 0.978 Å |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Aug 8, 2020 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→33 Å / Num. obs: 52113 / % possible obs: 96 % / Redundancy: 6.2 % / CC1/2: 0.99 / Rmerge(I) obs: 0.0118 / Net I/σ(I): 8 |
Reflection shell | Resolution: 2.1→2.16 Å / Rmerge(I) obs: 0.78 / Num. unique obs: 3363 / CC1/2: 0.55 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2IDX Resolution: 2.1→32.999 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 25.52 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 104.77 Å2 / Biso mean: 48.7034 Å2 / Biso min: 28.62 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.1→32.999 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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