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Open data
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Basic information
Entry | Database: PDB / ID: 8fjd | ||||||
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Title | Structure of chlorophyllase from Triticum aestivum | ||||||
![]() | Chlorophyllase | ||||||
![]() | PLANT PROTEIN / Alpha/Beta Hydrolase | ||||||
Function / homology | chlorophyllase / pheophytinase b activity / Chlorophyllase / Chlorophyllase / chlorophyll catabolic process / chlorophyllase activity / Alpha/Beta hydrolase fold / chlorophyllase![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Boggs, D. / Jo, M. / Bridwell-Rabb, J. | ||||||
Funding support | ![]()
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![]() | ![]() Title: A structure-function analysis of chlorophyllase reveals a mechanism for activity regulation dependent on disulfide bonds. Authors: Jo, M. / Knapp, M. / Boggs, D.G. / Brimberry, M. / Donnan, P.H. / Bridwell-Rabb, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 135.7 KB | Display | ![]() |
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PDB format | ![]() | 95.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 440 KB | Display | ![]() |
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Full document | ![]() | 462 KB | Display | |
Data in XML | ![]() | 25.4 KB | Display | |
Data in CIF | ![]() | 33.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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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: 34674.855 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-CA / | #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.93 Å3/Da / Density % sol: 68.71 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop Details: 0.2 M calcium acetate, 0.1 M sodium cacodylate (pH 6.5), 40% PEG300 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-300 / Detector: CCD / Date: Apr 7, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 4.46→50 Å / Num. obs: 6846 / % possible obs: 96.8 % / Redundancy: 12.57 % / Biso Wilson estimate: 124.89 Å2 / CC1/2: 0.995 / Net I/σ(I): 7.44 |
Reflection shell | Resolution: 4.46→4.62 Å / Num. unique obs: 684 / CC1/2: 0.996 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 129.93 Å2 | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 4.46→49.13 Å
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Refine LS restraints |
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LS refinement shell |
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