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Yorodumi- PDB-1typ: SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLU... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1typ | ||||||
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Title | SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLUTATHIONYLSPERMIDINE DISULPHIDE AT 0.28-NM RESOLUTION | ||||||
Components | TRYPANOTHIONE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE | ||||||
Function / homology | Function and homology information trypanothione-disulfide reductase / trypanothione-disulfide reductase (NADPH) activity / cell redox homeostasis / flavin adenine dinucleotide binding / cytoplasm Similarity search - Function | ||||||
Biological species | Crithidia fasciculata (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.8 Å | ||||||
Authors | Bailey, S. / Hunter, W.N. | ||||||
Citation | Journal: Eur.J.Biochem. / Year: 1993 Title: Substrate interactions between trypanothione reductase and N1-glutathionylspermidine disulphide at 0.28-nm resolution. Authors: Bailey, S. / Smith, K. / Fairlamb, A.H. / Hunter, W.N. #1: 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. / Abogye-Kwarteng, T. / Smith, K. / Fairlamb, A.H. #2: Journal: Science / Year: 1992 Title: Crystal Structures of Two Viral Peptides in Complex with Murine Mhc Class I H-2KB Authors: Fremont, D.H. / Matsumura, M. / Stura, E.A. / Peterson, P.A. / Wilson, I.A. #3: 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. #4: Journal: Nature / Year: 1984 Title: A Large Increase in Enzyme-Substrate Affinity by Protein Engineering Authors: Wilkinson, A.J. / Fersht, A.R. / Blow, D.M. / Carter, P. / Winter, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1typ.cif.gz | 206 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1typ.ent.gz | 172.5 KB | Display | PDB format |
PDBx/mmJSON format | 1typ.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ty/1typ ftp://data.pdbj.org/pub/pdb/validation_reports/ty/1typ | HTTPS FTP |
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-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 |
-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 52901.805 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 |
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-Non-polymers , 5 types, 412 molecules
#2: Chemical | #3: Chemical | #4: Chemical | ChemComp-GSH / #5: Chemical | ChemComp-SPD / #6: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | N1-GLUTATHION |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 66.07 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8.85 Å / Num. obs: 35848 / % possible obs: 70 % / Rmerge(I) obs: 0.096 |
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Reflection shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.95 Å / % possible obs: 36.9 % / Num. possible: 5076 / Rmerge(I) obs: 0.24 |
-Processing
Software |
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Refinement | Resolution: 2.8→8 Å / σ(F): 1 Details: REFERENCE 1 DESCRIBES THE STRUCTURE SOLUTION BY MOLECULAR REPLACEMENT AND PARTIAL REFINEMENT TO ALLOW DETAILS OF THE ACTIVE SITE TO BE PRESENTED.
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Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 8 Å / Num. reflection obs: 32393 / σ(F): 1 / Rfactor obs: 0.148 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.3 |