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Open data
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Basic information
Entry | Database: PDB / ID: 1lhs | ||||||
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Title | LOGGERHEAD SEA TURTLE MYOGLOBIN (AQUO-MET) | ||||||
![]() | MYOGLOBIN | ||||||
![]() | OXYGEN STORAGE | ||||||
Function / homology | ![]() nitrite reductase activity / Oxidoreductases; Acting on other nitrogenous compounds as donors / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / removal of superoxide radicals / oxygen carrier activity / oxygen binding / peroxidase activity / heme binding / extracellular exosome / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Nardini, M. / Tarricone, C. / Lania, A. / Desideri, A. / De Sanctis, G. / Coletta, M. / Petruzzelli, R. / Ascenzi, P. / Coda, A. / Bolognesi, M. | ||||||
![]() | ![]() Title: Reptile heme protein structure: X-ray crystallographic study of the aquo-met and cyano-met derivatives of the loggerhead sea turtle (Caretta caretta) myoglobin at 2.0 A resolution. Authors: Nardini, M. / Tarricone, C. / Rizzi, M. / Lania, A. / Desideri, A. / De Sanctis, G. / Coletta, M. / Petruzzelli, R. / Ascenzi, P. / Coda, A. / Bolognesi, M. #1: ![]() Title: X-Ray Crystal Structure of Aplysia Limacina Myoglobin in Different Liganded States Authors: Conti, E. / Moser, C. / Rizzi, M. / Mattevi, A. / Lionetti, C. / Coda, A. / Ascenzi, P. / Brunori, M. / Bolognesi, M. #2: ![]() Title: Structural Studies on the Loggerhead Sea Turtle (Caretta Caretta) Myoglobin Authors: Petruzzelli, R. / Aureli, G. / Casale, E. / Nardini, M. / Rizzi, M. / Ascenzi, P. / Coletta, M. / De Sanctis, G. / Desideri, A. / Galtieri, A. / Bolognesi, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 44.8 KB | Display | ![]() |
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PDB format | ![]() | 30.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 477.7 KB | Display | ![]() |
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Full document | ![]() | 484.6 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 8.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 17420.980 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-HEM / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.47 Å3/Da / Density % sol: 50.24 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8 / Method: vapor diffusion | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Oct 2, 1994 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 13820 / % possible obs: 97.7 % / Observed criterion σ(I): 3 / Redundancy: 4 % |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 15 Å / Num. measured all: 58570 / Rmerge(I) obs: 0.0365 |
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Processing
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Refinement | Resolution: 2→15 Å / σ(F): 3 /
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Refinement step | Cycle: LAST / Resolution: 2→15 Å
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Refine LS restraints | *PLUS
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