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- PDB-2xax: Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit o... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xax | |||||||||
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Title | Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit of E. coli | |||||||||
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![]() | OXIDOREDUCTASE / NUCLEOTIDE-BINDING / ALTERNATIVE INITIATION / DNA REPLICATION / ALLOSTERIC ENZYME | |||||||||
Function / homology | ![]() ribonucleoside diphosphate metabolic process / 2'-deoxyribonucleotide biosynthetic process / ribonucleoside-diphosphate reductase complex / nucleobase-containing small molecule interconversion / ribonucleoside-diphosphate reductase / ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor / deoxyribonucleotide biosynthetic process / protein folding chaperone / DNA replication / iron ion binding ...ribonucleoside diphosphate metabolic process / 2'-deoxyribonucleotide biosynthetic process / ribonucleoside-diphosphate reductase complex / nucleobase-containing small molecule interconversion / ribonucleoside-diphosphate reductase / ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor / deoxyribonucleotide biosynthetic process / protein folding chaperone / DNA replication / iron ion binding / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Yokoyama, K. / Uhlin, U. / Stubbe, J. | |||||||||
![]() | ![]() Title: Site-Specific Incorporation of 3-Nitrotyrosine as a Probe of Pk(A) Perturbation of Redox-Active Tyrosines in Ribonucleotide Reductase. Authors: Yokoyama, K. / Uhlin, U. / Stubbe, J. #1: ![]() Title: Structure of Ribonucleotide Reductase Protein R1 Authors: Uhlin, U. / Eklund, H. #2: ![]() Title: Binding of Allosteric Effectors to Ribonucleotide Reductase Protein R1: Reduction of Active-Site Cysteines Promotes Substrate Binding. Authors: Eriksson, M. / Uhlin, U. / Ramaswamy, S. / Ekberg, M. / Regnstrom, K. / Sjoberg, B.M. / Eklund, H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 451.1 KB | Display | ![]() |
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PDB format | ![]() | 370.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 498.2 KB | Display | ![]() |
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Full document | ![]() | 560.7 KB | Display | |
Data in XML | ![]() | 88.4 KB | Display | |
Data in CIF | ![]() | 122.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2x0xSC ![]() 2xakC ![]() 2xapC ![]() 2xavC ![]() 2xawC ![]() 2xayC ![]() 2xazC C: citing same article ( S: Starting model for refinement |
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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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2 | ![]()
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3 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 85829.992 Da / Num. of mol.: 3 / Fragment: RESIDUES 1-761 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00452, ribonucleoside-diphosphate reductase #2: Protein/peptide | Mass: 2271.392 Da / Num. of mol.: 4 Fragment: RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376 Source method: obtained synthetically / Source: (synth.) ![]() ![]() References: UniProt: P69924, ribonucleoside-diphosphate reductase #3: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, TYR 731 TO ALA ENGINEERED RESIDUE IN CHAIN B, TYR 731 TO ALA ...ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.17 Å3/Da / Density % sol: 54 % / Description: NONE |
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Crystal grow | pH: 6 Details: LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 15, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8726 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→84.21 Å / Num. obs: 75336 / % possible obs: 89.5 % / Observed criterion σ(I): -3.7 / Redundancy: 5.61 % / Rmerge(I) obs: 0.18 / Net I/σ(I): 9.83 |
Reflection shell | Resolution: 2.75→2.77 Å / Redundancy: 5.34 % / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 1.68 / % possible all: 87 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2X0X Resolution: 2.75→169.031 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.877 / SU B: 12.81 / SU ML: 0.255 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.385 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 268-273 ARE DISORDERED. THE 16 C-TERMINAL RESIDUES OF THE R2 PEPTIDE, CHAINS D, E, F, BIND AT THE R2 BINDING-SITE OF THE R1 ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 268-273 ARE DISORDERED. THE 16 C-TERMINAL RESIDUES OF THE R2 PEPTIDE, CHAINS D, E, F, BIND AT THE R2 BINDING-SITE OF THE R1 MOLECULES, CHAINS A, B, C. THE THREE N-TERMINAL RESIDUES, UNIQUE CHAIN P, ARE SITUATED BETWEEN MOL A AND C. THIS LATTER BINDING HAS NO KNOWN BIOLOGICAL RELEVANCE BUT IS NEEDED FOR CRYSTAL- LATTICE FORMATION. WATERS CLOSE TO SER 625 MAY REPRESENT A SULPHATE ION.
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Solvent computation | Ion probe radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 40.101 Å2
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Refinement step | Cycle: LAST / Resolution: 2.75→169.031 Å
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Refine LS restraints |
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