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- PDB-2hji: Structural model for the Fe-containing isoform of acireductone di... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2hji | ||||||
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Title | Structural model for the Fe-containing isoform of acireductone dioxygenase | ||||||
![]() | E-2/E-2' protein | ||||||
![]() | OXIDOREDUCTASE / dioxygenase / non-heme iron / isozyme / methionine salvage / structural entropy | ||||||
Function / homology | ![]() acireductone dioxygenase (Ni2+-requiring) / acireductone dioxygenase [iron(II)-requiring] / acireductone dioxygenase (Ni2+-requiring) activity / acireductone dioxygenase [iron(II)-requiring] activity / L-methionine salvage from S-adenosylmethionine / L-methionine salvage from methylthioadenosine / nickel cation binding / iron ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / restrained simulated annealing using torsional dynamics | ||||||
![]() | Pochapsky, T.C. / Ju, T. / Maroney, M.J. / Chai, S.C. | ||||||
![]() | ![]() Title: One Protein, Two Enzymes Revisited: A Structural Entropy Switch Interconverts the Two Isoforms of Acireductone Dioxygenase Authors: Ju, T. / Goldsmith, R.B. / Chai, S.C. / Maroney, M.J. / Pochapsky, S.S. / Pochapsky, T.C. #1: Journal: J.Biol.Chem. / Year: 1999 Title: One protein, two enzymes. Authors: Dai, Y. / Wensink, P. / Abeles, R.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 674.9 KB | Display | ![]() |
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PDB format | ![]() | 561 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 347.1 KB | Display | ![]() |
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Full document | ![]() | 506.1 KB | Display | |
Data in XML | ![]() | 57.6 KB | Display | |
Data in CIF | ![]() | 75.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 20219.412 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q9ZFE7, acireductone dioxygenase [iron(II)-requiring] |
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#2: Chemical | ChemComp-FE2 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: residual dipolar couplings obtained using filamentous phage (fd) and C12E5 polyol |
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Sample preparation
Details | Contents: uniform 15N, 13C labeled, 1 mM / Solvent system: 90/10 H2O/D2O 50 mM KPi buffer, pH 7.5 |
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Sample conditions | Ionic strength: 50 mM KPi / pH: 7.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
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Processing
NMR software | Name: CNS / Developer: Brunger A. T. etall / Classification: refinement |
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Refinement | Method: restrained simulated annealing using torsional dynamics Software ordinal: 1 Details: Only residues 1-156 are included in structural models, as residues 157-179 are disordered in solution. |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: back calculated data agree with experimental NOESY spectrum,structures with acceptable covalent geometry Conformers calculated total number: 300 / Conformers submitted total number: 14 |