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- PDB-1feb: UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1feb | ||||||
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Title | UNLIGANDED CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.0 ANGSTROM RESOLUTION | ||||||
![]() | TRYPANOTHIONE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / REDOX-ACTIVE CENTER / FLAVOPROTEIN / FAD / NADP | ||||||
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 | ![]() | ||||||
![]() | Strickland, C. / Karplus, P. | ||||||
![]() | ![]() Title: Crithidia Fasciculata Trypanothione Reductase at 1.70 A Resolution Authors: Strickland, C.L. / Karplus, P.A. #1: ![]() Title: Overexpression of Crithidia Fasciculata Trypanothione Reductase and Crystallization Using a Novel Geometry Authors: Strickland, C. / Puchalski, R. / Savvides, S. / Karplus, P. #2: ![]() Title: Structure of Trypanothione Reductase from Crithidia Fasciculata at 2.6 A Resolution: Enzyme-Nadp Interactions of 2.8 A Resolution Authors: Bailey, S. / Fairlamb, A. / Hunter, W. #3: ![]() Title: The Structure of Trypanosoma Cruzi Trypanothione Reductase in the Oxidized and Nadph Reduced State Authors: Lantwin, C.B. / Schlichting, I. / Kabsch, W. / Pai, E.F. / Krauth-Siegel, R.L. #4: ![]() 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. #5: ![]() Title: X-Ray Structure of Trypanothione Reductase from Crithidia Fasciculata at 2.4-A Resolution Authors: Kuriyan, J. / Kong, X.P. / Krishna, T.S. / Sweet, R.M. / Murgolo, N.J. / Field, H. / Cerami, A. / Henderson, G.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198.4 KB | Display | ![]() |
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PDB format | ![]() | 164.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 955.1 KB | Display | ![]() |
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Full document | ![]() | 976.6 KB | Display | |
Data in XML | ![]() | 40.5 KB | Display | |
Data in CIF | ![]() | 57.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 53176.008 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ORTHORHOMBIC CRYSTAL FORM, DIMER IN THE ASYMMETRIC UNIT Source: (gene. exp.) ![]() Description: SEE STRICKLAND, ET. AL. (1995) ACTA CRYST. D51, 337-341 Gene: TR1 / Plasmid: PET-TR1 / Gene (production host): TR1 / Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 53 % |
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Mar 5, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 69192 / % possible obs: 89 % / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Rmerge(I) obs: 0.119 |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 1 /
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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