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Yorodumi- PDB-2mhr: STRUCTURE OF MYOHEMERYTHRIN IN THE AZIDOMET STATE AT 1.7(SLASH)1.... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mhr | |||||||||
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Title | STRUCTURE OF MYOHEMERYTHRIN IN THE AZIDOMET STATE AT 1.7(SLASH)1.3 ANGSTROMS RESOLUTION | |||||||||
Components | MYOHEMERYTHRIN | |||||||||
Keywords | OXYGEN BINDING | |||||||||
Function / homology | Function and homology information inorganic ion homeostasis / monoatomic cation homeostasis / oxygen carrier activity / iron ion binding Similarity search - Function | |||||||||
Biological species | Themiste zostericola (invertebrata) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 1.3 Å | |||||||||
Authors | Sheriff, S. / Hendrickson, W.A. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1987 Title: Structure of myohemerythrin in the azidomet state at 1.7/1.3 A resolution. Authors: Sheriff, S. / Hendrickson, W.A. / Smith, J.L. #1: Journal: Acta Crystallogr.,Sect.B / Year: 1987 Title: Location of Iron and Sulfur Atoms in Myohemerythrin from Anomalous-Scattering Measurements Authors: Sheriff, S. / Hendrickson, W.A. #2: Journal: Acta Crystallogr.,Sect.A / Year: 1987 Title: General Density Function Corresponding to X-Ray Diffraction with Anomalous Scattering Included Authors: Hendrickson, W.A. / Sheriff, S. #3: Journal: Acta Crystallogr.,Sect.A / Year: 1987 Title: Description of Overall Anisotropy in Diffraction from Macromolecular Crystals Authors: Sheriff, S. / Hendrickson, W.A. #4: Journal: Biochemistry / Year: 1986 Title: Structural Heterogeneity in Protein Crystals Authors: Smith, J.L. / Hendrickson, W.A. / Honzatko, R.B. / Sheriff, S. #5: Journal: Biomolecular Stereodynamics III. Proceedings of the Fourth Conversation in the Discipline of Biomolecular Stereodynamics Year: 1986 Title: Mobility and Heterogeneity in Protein Structure as Seen by Diffraction Authors: Hendrickson, W.A. / Smith, J.L. / Sheriff, S. #6: Journal: Proc.Natl.Acad.Sci.USA / Year: 1985 Title: Influence of Solvent Accessibility and Intermolecular Contacts on Atomic Mobilities in Hemerythrins Authors: Sheriff, S. / Hendrickson, W.A. / Stenkamp, R.E. / Sieker, L.C. / Jensen, L.H. #7: Journal: Respiratory Pigments in Animals / Year: 1985 Title: Structure and Function of Hemerythrins Authors: Hendrickson, W.A. / Smith, J.L. / Sheriff, S. #8: Journal: Life Chem.Rep.,Suppl.Ser. / Year: 1983 Title: Structure of the Active Center of Hemerythrins Authors: Sheriff, S. / Hendrickson, W.A. / Smith, J.L. #9: Journal: Proc.Natl.Acad.Sci.USA / Year: 1975 Title: Tertiary Structure of Myohemerythrin at Low Resolution Authors: Hendrickson, W.A. / Klippenstein, G.L. / Ward, K.B. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mhr.cif.gz | 59.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mhr.ent.gz | 49.1 KB | Display | PDB format |
PDBx/mmJSON format | 2mhr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mh/2mhr ftp://data.pdbj.org/pub/pdb/validation_reports/mh/2mhr | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO 7 AND PRO 90 ARE CIS PROLINES. |
-Components
#1: Protein | Mass: 13800.746 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Themiste zostericola (invertebrata) / References: UniProt: P02247 | ||||||
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#2: Chemical | ChemComp-AZI / | ||||||
#3: Chemical | #4: Chemical | ChemComp-FEO / | #5: Water | ChemComp-HOH / | Compound details | THERE ARE TWO TURNS IN MYOHEMERYTHRIN WHICH INVOLVE A QUINTET OF RESIDUES AND ARE NOT WELL ...THERE ARE TWO TURNS IN MYOHEMERYT | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.23 % | |||||||||||||||
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Crystal grow | *PLUS pH: 6.7 / Method: unknown / Details: seeding | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS |
-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.3→10 Å / Rfactor obs: 0.158 / σ(F): 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refine analyze | Luzzati coordinate error obs: 0.14 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.3→10 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 16654 / σ(I): 2 / Highest resolution: 1.3 Å / Lowest resolution: 1.7 Å / Rfactor obs: 0.158 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |