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- PDB-2tpr: X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2tpr | ||||||
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Title | X-RAY STRUCTURE OF TRYPANOTHIONE REDUCTASE FROM CRITHIDIA FASCICULATA AT 2.4 ANGSTROMS 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 | ![]() | ||||||
![]() | Kuriyan, J. / Kong, X.-P. / Krishna, T.S.R. | ||||||
![]() | ![]() 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. #1: ![]() Title: Preliminary Crystallographic Analysis of Trypanothione Reductase from Crithidia Fasciculata Authors: Kuriyan, J. / Wong, L. / Guenther, B.D. / Murgolo, N.J. / Cerami, A. / Henderson, G.B. #2: ![]() Title: Purification and Characterization of Trypanothione Reductase from Crithidia Fasciculata, a Newly Discovered Member of the Family of Disulfide-Containing Flavoprotein Reductases Authors: Shames, S.L. / Fairlamb, A.H. / Cerami, A. / Walsh, C.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 202.8 KB | Display | ![]() |
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PDB format | ![]() | 161.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 947.7 KB | Display | ![]() |
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Full document | ![]() | 970.7 KB | Display | |
Data in XML | ![]() | 40.9 KB | Display | |
Data in CIF | ![]() | 57.6 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 42 / 2: CIS PROLINE - PRO A 369 / 3: CIS PROLINE - PRO A 461 / 4: CIS PROLINE - PRO B 42 / 5: CIS PROLINE - PRO B 369 / 6: CIS PROLINE - PRO B 461 |
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Components
#1: Protein | Mass: 53127.965 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.84 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 42201 / % possible obs: 88 % / Num. measured all: 131449 / Rmerge(I) obs: 0.079 |
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Processing
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Refinement | Rfactor Rwork: 0.18 / Rfactor obs: 0.18 / Highest resolution: 2.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 6 Å / Num. reflection obs: 33134 / σ(F): 2 / Rfactor obs: 0.18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.7 |