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Open data
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Basic information
Entry | Database: PDB / ID: 1ezk | ||||||
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Title | Crystal structure of recombinant tryparedoxin I | ||||||
![]() | TRYPAREDOXIN I | ||||||
![]() | ELECTRON TRANSPORT | ||||||
Function / homology | ![]() thioredoxin-disulfide reductase (NADPH) activity / negative regulation of Wnt signaling pathway / negative regulation of protein ubiquitination / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hofmann, B. / Guerrero, S.A. / Kalisz, H.M. / Menge, U. / Nogoceke, E. / Montemartini, M. / Singh, M. / Flohe, L. / Hecht, H.J. | ||||||
![]() | ![]() Title: Structures of tryparedoxins revealing interaction with trypanothione. Authors: Hofmann, B. / Budde, H. / Bruns, K. / Guerrero, S.A. / Kalisz, H.M. / Menge, U. / Montemartini, M. / Nogoceke, E. / Steinert, P. / Wissing, J.B. / Flohe, L. / Hecht, H.J. #1: ![]() Title: Sequence, Heterologous Expression and Functional Characterization of Tryparedoxin I from Crithidias fasciculata | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 42.3 KB | Display | ![]() |
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PDB format | ![]() | 32.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.9 KB | Display | ![]() |
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Full document | ![]() | 432.5 KB | Display | |
Data in XML | ![]() | 10.6 KB | Display | |
Data in CIF | ![]() | 14.6 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: 17438.588 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: C-TERMINAL HIS-TAG / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.82 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: PEG 4000, Tris, Mes, sodium acetate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 292K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 294 KDetails: Kalisz, H.M., (1998) Acta Crystallogr., Sect.D, 55, 696. pH: 8.7 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 13, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→27.5 Å / Num. all: 11980 / Num. obs: 11980 / % possible obs: 96.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.1 % / Biso Wilson estimate: 23.25 Å2 / Rmerge(I) obs: 0.079 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.128 / Num. unique all: 1417 / % possible all: 81.1 |
Reflection | *PLUS Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 1.9→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→50 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 50 Å / σ(F): 0 / Rfactor obs: 0.198 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |