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- PDB-4rxn: CRYSTALLOGRAPHIC REFINEMENT OF RUBREDOXIN AT 1.2 ANGSTROMS RESOLUTION -
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Open data
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Basic information
Entry | Database: PDB / ID: 4rxn | |||||||||
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Title | CRYSTALLOGRAPHIC REFINEMENT OF RUBREDOXIN AT 1.2 ANGSTROMS RESOLUTION | |||||||||
![]() | RUBREDOXIN | |||||||||
![]() | ELECTRON TRANSFER(IRON-SULFUR PROTEIN) | |||||||||
Function / homology | ![]() alkane catabolic process / electron transfer activity / iron ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Watenpaugh, K.D. / Sieker, L.C. / Jensen, L.H. | |||||||||
![]() | ![]() Title: Crystallographic refinement of rubredoxin at 1 x 2 A degrees resolution. Authors: Watenpaugh, K.D. / Sieker, L.C. / Jensen, L.H. #1: ![]() Title: The Structure of Rubredoxin at 1.2 Angstroms Resolution Authors: Watenpaugh, K.D. / Sieker, L.C. / Jensen, L.H. #2: ![]() Title: Water Structure in a Protein Crystal. Rubredoxin at 1.2 Angstroms Resolution. Authors: Watenpaugh, K.D. / Margulis, T.N. / Sieker, L.C. / Jensen, L.H. #3: ![]() Title: Refinement of the Model of a Protein. Rubredoxin at 1.5 Angstroms Resolution Authors: Watenpaugh, K.D. / Sieker, L.C. / Herriott, J.R. / Jensen, L.H. #4: ![]() Title: Sequence of Rubredoxin by X-Ray Diffraction Authors: Herriott, J.R. / Watenpaugh, K.D. / Sieker, L.C. / Jensen, L.H. #5: ![]() Title: The Structure of a Non-Heme Iron Protein, Rubredoxin at 1.5 Angstroms Resolution Authors: Watenpaugh, K.D. / Sieker, L.C. / Herriott, J.R. / Jensen, L.H. #6: ![]() Title: The Primary Structure of Clostridium Pasteurianum Rubredoxin Authors: Mccarthy, K.F. #7: ![]() Title: Structure of Rubredoxin. An X-Ray Study to 2.5 Angstroms Resolution Authors: Herriott, J.R. / Sieker, L.C. / Jensen, L.H. / Lovenberg, W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.9 KB | Display | ![]() |
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PDB format | ![]() | 26.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 372.2 KB | Display | ![]() |
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Full document | ![]() | 405.1 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Data in CIF | ![]() | 9.8 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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Unit cell |
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Components
#1: Protein | Mass: 6054.566 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-FE / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42.32 % |
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Crystal grow | *PLUS Temperature: 23 ℃ / pH: 4 / Method: unknown / Details: salting out |
Components of the solutions | *PLUS Conc.: 80 %sat / Chemical formula: (NH4)2SO4 |
-Data collection
Reflection | *PLUS Observed criterion σ(I): 4 / Num. measured all: 17000 / Rmerge(I) obs: 0.038 |
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Processing
Refinement | Resolution: 1.2→10 Å Details: EACH HYDROGEN ATOM POSITION HAS BEEN CALCULATED FROM THE COORDINATES OF THE ATOM IT IS BONDED TO. THE B-VALUE OF THE HEAVIER ATOM WAS ASSIGNED TO THE HYDROGEN ATOM. THE CELL DIMENSIONS ...Details: EACH HYDROGEN ATOM POSITION HAS BEEN CALCULATED FROM THE COORDINATES OF THE ATOM IT IS BONDED TO. THE B-VALUE OF THE HEAVIER ATOM WAS ASSIGNED TO THE HYDROGEN ATOM. THE CELL DIMENSIONS VARIED FROM START TO FINISH OF DATA COLLECTION. THE VALUES GIVEN ARE THOSE AT THE MID-POINT OF DATA COLLECTION.
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Refinement step | Cycle: LAST / Resolution: 1.2→10 Å
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Refinement | *PLUS Highest resolution: 1.2 Å / Lowest resolution: 10 Å / Num. reflection obs: 10936 / σ(I): 2 / Rfactor obs: 0.128 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 12 Å2 |