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Yorodumi- PDB-8qpj: FAD-independent Methylene-Tetrahydrofolate Reductase Mutant E9Q f... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8qpj | ||||||
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Title | FAD-independent Methylene-Tetrahydrofolate Reductase Mutant E9Q from Mycobacterium hassiacum | ||||||
Components | Methylenetetrahydrofolate reductase (NAD(P)H) | ||||||
Keywords | OXIDOREDUCTASE / Methylenetetrahydrofolate reductase / methylene-tetrahydrofolate reductase | ||||||
Function / homology | Mycobacterial methylenetetrahydrofolate reductase / Methylenetetrahydrofolate reductase (NAD(P)H) Function and homology information | ||||||
Biological species | Mycolicibacterium hassiacum (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å | ||||||
Authors | Gehl, M. / Demmer, U. / Ermler, U. / Shima, S. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Protein Sci. / Year: 2024 Title: Mutational and structural studies of ( beta alpha ) 8 -barrel fold methylene-tetrahydropterin reductases utilizing a common catalytic mechanism. Authors: Gehl, M. / Demmer, U. / Ermler, U. / Shima, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8qpj.cif.gz | 337.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8qpj.ent.gz | 276.7 KB | Display | PDB format |
PDBx/mmJSON format | 8qpj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8qpj_validation.pdf.gz | 434.2 KB | Display | wwPDB validaton report |
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Full document | 8qpj_full_validation.pdf.gz | 439.7 KB | Display | |
Data in XML | 8qpj_validation.xml.gz | 24.9 KB | Display | |
Data in CIF | 8qpj_validation.cif.gz | 36 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qp/8qpj ftp://data.pdbj.org/pub/pdb/validation_reports/qp/8qpj | HTTPS FTP |
-Related structure data
Related structure data | 8qplC 8qpmC 8qq8C C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-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
#1: Protein | Mass: 32836.695 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycolicibacterium hassiacum (bacteria) / Gene: C731_4202 / Production host: Escherichia coli (E. coli) / References: UniProt: K5BDY6 #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: 2.03 Å3/Da / Density % sol: 39.5 % |
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Crystal grow | Temperature: 281 K / Method: vapor diffusion, sitting drop Details: 25 % PEG MME 5000 10 mg/ml Mfr_E9Q 2 mM NAD+ 2 mM CH3-H4F |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 25, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→45.8 Å / Num. obs: 51871 / % possible obs: 98.7 % / Redundancy: 3.3 % / CC1/2: 0.997 / Rmerge(I) obs: 0.088 / Net I/σ(I): 8.17 |
Reflection shell | Resolution: 1.75→1.813 Å / Rmerge(I) obs: 1.05 / Num. unique obs: 5183 / CC1/2: 0.431 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.75→45.8 Å / Cross valid method: FREE R-VALUE
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Refinement step | Cycle: LAST / Resolution: 1.75→45.8 Å
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