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Yorodumi- PDB-1tyt: CRYSTAL AND MOLECULAR STRUCTURE OF CRITHIDIA FASCICULATA TRYPANOT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tyt | ||||||
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Title | CRYSTAL AND MOLECULAR STRUCTURE OF CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.6 ANGSTROMS RESOLUTION | ||||||
Components | TRYPANOTHIONE REDUCTASE, OXIDIZED FORM | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information trypanothione-disulfide reductase / trypanothione-disulfide reductase (NADPH) activity / glutathione-disulfide reductase (NADPH) activity / glutathione metabolic process / cell redox homeostasis / flavin adenine dinucleotide binding / cellular response to oxidative stress / mitochondrion / cytosol Similarity search - Function | ||||||
Biological species | Crithidia fasciculata (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Bailey, S. / Hunter, W.N. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 1994 Title: Structure of trypanothione reductase from Crithidia fasciculata at 2.6 A resolution; enzyme-NADP interactions at 2.8 A resolution. Authors: Bailey, S. / Fairlamb, A.H. / Hunter, W.N. #1: Journal: Eur.J.Biochem. / Year: 1993 Title: Substrate Interactions between Trypanothione Reductase and N1-Glutathionyldisulphide at 2.8 Angstroms Resolution Authors: Bailey, S. / Smith, K. / Fairlamb, A.H. / Hunter, W.N. #2: Journal: J.Mol.Biol. / Year: 1992 Title: Active Site of Trypanothione Reductase: A Target for Rational Drug Design Authors: Hunter, W.N. / Bailey, S. / Habash, J. / Harrop, S.J. / Helliwell, J.R. / Aboagye-Kwarteng, T. / Smith, K. / Fairlamb, A.H. #3: Journal: Mol.Microbiol. / Year: 1992 Title: Molecular Characterization of the Trypanothione Reductase Gene from Crithidia Fasciculata and Trypanosoma Brucei: Comparison with Other Flavo Protein Disulphide Oxidoreductases with Respect to ...Title: Molecular Characterization of the Trypanothione Reductase Gene from Crithidia Fasciculata and Trypanosoma Brucei: Comparison with Other Flavo Protein Disulphide Oxidoreductases with Respect to Substrate Specificity and Catalytic Mechanism Authors: Aboagye-Kwarteng, T. / Smith, K. / Fairlamb, A.H. #4: Journal: J.Mol.Biol. / Year: 1990 Title: Initiating a Crystallographic Study of Trypanothione Reductase Authors: Hunter, W.N. / Smith, K. / Derewenda, Z. / Harrop, S.J. / Habash, J. / Islam, M.S. / Helliwell, J.R. / Fairlamb, A.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tyt.cif.gz | 204.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tyt.ent.gz | 161.9 KB | Display | PDB format |
PDBx/mmJSON format | 1tyt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tyt_validation.pdf.gz | 944.5 KB | Display | wwPDB validaton report |
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Full document | 1tyt_full_validation.pdf.gz | 977.5 KB | Display | |
Data in XML | 1tyt_validation.xml.gz | 43.2 KB | Display | |
Data in CIF | 1tyt_validation.cif.gz | 60.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ty/1tyt ftp://data.pdbj.org/pub/pdb/validation_reports/ty/1tyt | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 43 / 2: CIS PROLINE - PRO A 370 / 3: CIS PROLINE - PRO A 462 / 4: CIS PROLINE - PRO B 43 / 5: CIS PROLINE - PRO B 370 / 6: CIS PROLINE - PRO B 462 | ||||||||
Details | TRYPANOTHIONE REDUCTASE IS ACTIVE AS A DIMER OF TWO IDENTICAL SUBUNITS, WHICH HAVE BEEN ASSIGNED CHAIN IDENTIFIERS A AND B. |
-Components
#1: Protein | Mass: 52862.770 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Crithidia fasciculata (eukaryote) / References: UniProt: P39040, EC: 1.6.4.8 #2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | THERE IS ONE DISCREPANCY BETWEEN THE CRYSTAL STRUCTURE AND THE AMINO ACID SEQUENCE DEDUCED FROM THE ...THERE IS ONE DISCREPANC | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.63 Å3/Da / Density % sol: 66.09 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 278 K / Method: vapor diffusion, sitting drop / pH: 7 | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 39038 / % possible obs: 83.5 % |
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-Processing
Software |
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Refinement | Resolution: 2.6→8 Å / Rfactor Rwork: 0.161 / Rfactor obs: 0.161 / σ(F): 1 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
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Software | *PLUS Name: X-PLOR / Classification: refinement | |||||||||||||||
Refinement | *PLUS Num. reflection obs: 35000 / Rfactor obs: 0.161 / Rfactor Rwork: 0.161 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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