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Open data
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Basic information
Entry | Database: PDB / ID: 1apx | ||||||
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Title | CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE | ||||||
![]() | CYTOSOLIC ASCORBATE PEROXIDASE | ||||||
![]() | PEROXIDASE | ||||||
Function / homology | ![]() L-ascorbate peroxidase / L-ascorbate peroxidase activity / chloroplast / response to reactive oxygen species / hydrogen peroxide catabolic process / cellular response to oxidative stress / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Patterson, W.R. / Poulos, T.L. | ||||||
![]() | ![]() Title: Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Authors: Patterson, W.R. / Poulos, T.L. #1: ![]() Title: Characterization and Crystallization of Recombinant Pea Cytosolic Ascorbate Peroxidase Authors: Patterson, W.R. / Poulos, T.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 216.4 KB | Display | ![]() |
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PDB format | ![]() | 173.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.8 MB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 45.1 KB | Display | |
Data in CIF | ![]() | 63.6 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 A 2 .. A 250 B 2 .. B 250 0.321 M2 A 2 .. A 250 C 2 .. C 250 0.347 M3 A 2 .. A 250 D 2 .. D 250 0.280 |
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Components
#1: Protein | Mass: 27097.561 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-K / #3: Chemical | ChemComp-HEM / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.36 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 25 ℃ / pH: 8.5 / Method: vapor diffusion, hanging drop / Details: or 7 degrees centigrade | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR / Date: Apr 8, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 1.9 Å / Num. obs: 65092 / % possible obs: 72 % / Observed criterion σ(I): 2 / Redundancy: 2.6 % |
Reflection | *PLUS Lowest resolution: 9999 Å |
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Processing
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Refinement | Resolution: 2.2→8 Å / σ(F): 2 Details: THE ALA 250 RESIDUES, PLUS THE C-TERMINAL CARBOXYL GROUP, WERE ROUGHLY MODELED INTO POOR, BUT OBSERVABLE, DENSITY.
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.279 |