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Open data
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Basic information
Entry | Database: PDB / ID: 1qoa | ||||||
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Title | FERREDOXIN MUTATION C49S | ||||||
![]() | FERREDOXIN | ||||||
![]() | ELECTRON TRANSPORT / IRON-SULFUR / FERREDOXIN | ||||||
Function / homology | ![]() electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Holden, H.M. / Benning, M.M. | ||||||
![]() | ![]() Title: Iron-sulfur cluster cysteine-to-serine mutants of Anabaena -2Fe-2S- ferredoxin exhibit unexpected redox properties and are competent in electron transfer to ferredoxin:NADP+ reductase. Authors: Hurley, J.K. / Weber-Main, A.M. / Hodges, A.E. / Stankovich, M.T. / Benning, M.M. / Holden, H.M. / Cheng, H. / Xia, B. / Markley, J.L. / Genzor, C. / Gomez-Moreno, C. / Hafezi, R. / Tollin, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.4 KB | Display | ![]() |
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PDB format | ![]() | 37.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 384.5 KB | Display | ![]() |
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Full document | ![]() | 389 KB | Display | |
Data in XML | ![]() | 5.6 KB | Display | |
Data in CIF | ![]() | 8.8 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 10689.559 Da / Num. of mol.: 2 / Mutation: C49S Source method: isolated from a genetically manipulated source Details: 2FE-2S FERREDOXIN / 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: 2.5 Å3/Da / Density % sol: 50.77 % | ||||||||||||||||||||
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Crystal grow | pH: 5.5 / Details: pH 5.5 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→25 Å / Num. obs: 20715 / % possible obs: 84.7 % / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.029 / Net I/σ(I): 27.8 |
Reflection shell | Resolution: 1.7→1.78 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.105 / Mean I/σ(I) obs: 4.2 / % possible all: 66 |
Reflection | *PLUS Num. obs: 21258 / % possible obs: 85 % / Num. measured all: 58282 |
Reflection shell | *PLUS % possible obs: 66 % / Num. unique obs: 2175 / Num. measured obs: 3478 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: WILD TYPE Resolution: 1.7→25 Å
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Refinement step | Cycle: LAST / Resolution: 1.7→25 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 20713 / Rfactor obs: 0.182 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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