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- PDB-1usp: Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans -
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Open data
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Basic information
Entry | Database: PDB / ID: 1usp | ||||||
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Title | Organic Hydroperoxide Resistance Protein from Deinococcus radiodurans | ||||||
![]() | (ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN) x 2 | ||||||
![]() | OXIDOREDUCTASE / 2-CYS PEROXIDASE | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Meunier-Jamin, C. / Kapp, U. / Leonard, G. / McSweeney, S. | ||||||
![]() | ![]() Title: The Structure of the Organic Hydroperoxide Resistance Protein from Deinococcus Radiodurans: Do Conformational Changes Facilitate Recycling of the Redox Disulfide? Authors: Meunier-Jamin, C. / Kapp, U. / Leonard, G. / Mcsweeney, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 59.5 KB | Display | ![]() |
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PDB format | ![]() | 47.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.8 KB | Display | ![]() |
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Full document | ![]() | 448.3 KB | Display | |
Data in XML | ![]() | 13.7 KB | Display | |
Data in CIF | ![]() | 18.6 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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.816, -0.565, 0.122), Vector: |
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Components
#1: Protein | Mass: 14686.871 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: R1 / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 14672.844 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: R1 / Production host: ![]() ![]() | ||
#3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 42 % |
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Crystal grow | pH: 7.2 / Details: pH 7.20 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→49.4 Å / Num. obs: 18043 / % possible obs: 91 % / Redundancy: 3.1 % / Biso Wilson estimate: 23.1 Å2 / Rmerge(I) obs: 0.054 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.309 / Mean I/σ(I) obs: 2.4 / % possible all: 62.5 |
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Processing
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Refinement | Method to determine structure: ![]() Details: IN BOTH MOLECULES MAKING UP THE HOMODIMER, ARG15 HAS BEEN AND MODELLED AS ALA, ALA16 AS GLY AND THE SIDE-CHAINS OF LYS70 GLU108 IN BOTH MOLECULES HAVE BEEN TRUNCATED AT THE CG ATOM. ...Details: IN BOTH MOLECULES MAKING UP THE HOMODIMER, ARG15 HAS BEEN AND MODELLED AS ALA, ALA16 AS GLY AND THE SIDE-CHAINS OF LYS70 GLU108 IN BOTH MOLECULES HAVE BEEN TRUNCATED AT THE CG ATOM. ADDITIONALLY, THE SIDE-CHAINS OF ILE71A, ASP76A, GLU139A AND LYS87B HAVE BEEN TRUNCATED AT CB. ILE71B HAS BEEN TRUNCATED AT CG2, ARG107B AT CG. GLU69B HAS BEEN MODELLED AS ASN
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Displacement parameters | Biso mean: 30.7 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→49.4 Å
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