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- PDB-6i93: R2-like ligand-binding oxidase G68L mutant with aerobically recon... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6i93 | ||||||
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Title | R2-like ligand-binding oxidase G68L mutant with aerobically reconstituted Fe/Fe cofactor | ||||||
![]() | Ribonucleotide reductase small subunit | ||||||
![]() | OXIDOREDUCTASE / R2-LIKE LIGAND-BINDING OXIDASE / MN/FE COFACTOR / RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FOLD / METALLOPROTEIN OXIDOREDUCTASE | ||||||
Function / homology | ![]() deoxyribonucleotide biosynthetic process / oxidoreductase activity / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Griese, J.J. / Hogbom, M. | ||||||
![]() | ![]() Title: Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins. Authors: Kutin, Y. / Kositzki, R. / Branca, R.M.M. / Srinivas, V. / Lundin, D. / Haumann, M. / Hogbom, M. / Cox, N. / Griese, J.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 | ![]() | 126 KB | Display | ![]() |
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PDB format | ![]() | 98.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6i90C ![]() 6i92C ![]() 6i94C ![]() 6i95C ![]() 4hr0S S: Starting model for refinement C: citing same article ( |
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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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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 37018.910 Da / Num. of mol.: 1 / Mutation: G68L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: HTA426 / Gene: GK2771 / Plasmid: pET-46 Ek/LIC / Production host: ![]() ![]() References: UniProt: Q5KW80, ribonucleoside-diphosphate reductase | ||||
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#2: Chemical | #3: Chemical | ChemComp-OCA / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.62 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 / Details: 27.5% (W/V) PEG 1500, 0.1 M HEPES-NA PH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 10, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 20702 / % possible obs: 99.7 % / Observed criterion σ(I): -3 / Redundancy: 4.1 % / Biso Wilson estimate: 36.6 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.059 / Rrim(I) all: 0.068 / Net I/σ(I): 17.98 |
Reflection shell | Resolution: 2.1→2.23 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.87 / Mean I/σ(I) obs: 1.63 / Num. unique obs: 3264 / CC1/2: 0.613 / Rrim(I) all: 1.002 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4HR0 Resolution: 2.101→27.964 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 2 / Phase error: 21.93
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.101→27.964 Å
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Refine LS restraints |
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LS refinement shell |
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