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Open data
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Basic information
Entry | Database: PDB / ID: 1rw4 | ||||||
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Title | Nitrogenase Fe protein l127 deletion variant | ||||||
![]() | Nitrogenase iron protein 1 | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sen, S. / Igarashi, R. / Smith, A. / Johnson, M.K. / Seefeldt, L.C. / Peters, J.W. | ||||||
![]() | ![]() Title: A Conformational Mimic of the MgATP-Bound "On State" of the Nitrogenase Iron Protein. Authors: Sen, S. / Igarashi, R. / Smith, A. / Johnson, M.K. / Seefeldt, L.C. / Peters, J.W. | ||||||
History |
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Remark 600 | HETEROGEN The iron cluster [4Fe-4S]2+ undergoes glycerol-induced cleavage to give rise to two [2Fe- ...HETEROGEN The iron cluster [4Fe-4S]2+ undergoes glycerol-induced cleavage to give rise to two [2Fe-2S] fragments. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.8 KB | Display | ![]() |
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PDB format | ![]() | 48.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1g20S S: Starting model for refinement |
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Similar 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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Components
#1: Protein | Mass: 29574.041 Da / Num. of mol.: 1 / Mutation: Leu127deletion Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SF4 / ![]() |
#3: Chemical | ChemComp-GOL / ![]() |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.43 Å3/Da / Density % sol: 49.41 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 8.5 / Method: batch method | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.5→20 Å / Num. obs: 10015 |
Reflection | *PLUS Highest resolution: 2.5 Å / % possible obs: 99.4 % / Num. measured all: 122724 / Rmerge(I) obs: 0.059 |
Reflection shell | *PLUS Rmerge(I) obs: 0.135 / Mean I/σ(I) obs: 4.7 |
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Processing
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Refinement | Method to determine structure![]() ![]() Starting model: 1G20 Resolution: 2.5→8 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree![]() ![]() | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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