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- PDB-1typ: SUBSTRATE INTERACTIONS BETWEEN TRYPANOTHIONE REDUCTASE AND N1-GLU... -
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Open data
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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 | ||||||
![]() | TRYPANOTHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() | ||||||
![]() | Bailey, S. / Hunter, W.N. | ||||||
![]() | ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 213.3 KB | Display | ![]() |
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PDB format | ![]() | 168.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.5 MB | Display | ![]() |
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Full document | ![]() | 2.6 MB | Display | |
Data in XML | ![]() | 46.2 KB | Display | |
Data in CIF | ![]() | 63.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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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 |
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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.) ![]() |
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-Non-polymers , 5 types, 412 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/GSH.gif)
![](data/chem/img/SPD.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/GSH.gif)
![](data/chem/img/SPD.gif)
![](data/chem/img/HOH.gif)
#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: ![]() |
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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 |
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Processing
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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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 |