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Yorodumi- PDB-1mni: ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mni | ||||||
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Title | ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN. BIS-IMIDAZOLE LIGATION IN THE HIS64-->VAL(SLASH)VAL68-->HIS DOUBLE MUTANT | ||||||
Components | MYOGLOBIN | ||||||
Keywords | OXYGEN STORAGE | ||||||
Function / homology | Function and homology information Intracellular oxygen transport / nitrite reductase activity / Oxidoreductases; Acting on other nitrogenous compounds as donors / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / oxygen transport / removal of superoxide radicals / peroxidase activity / oxygen carrier activity / oxygen binding ...Intracellular oxygen transport / nitrite reductase activity / Oxidoreductases; Acting on other nitrogenous compounds as donors / sarcoplasm / Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases / oxygen transport / removal of superoxide radicals / peroxidase activity / oxygen carrier activity / oxygen binding / heme binding / metal ion binding Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.07 Å | ||||||
Authors | Krzywda, S. / Wilkinson, A.J. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1995 Title: Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant. Authors: Dou, Y. / Admiraal, S.J. / Ikeda-Saito, M. / Krzywda, S. / Wilkinson, A.J. / Li, T. / Olson, J.S. / Prince, R.C. / Pickering, I.J. / George, G.N. #1: Journal: Biochemistry / Year: 1993 Title: Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of Threonine68(E11) Mutant Investigated by X-Ray Crystallography and Infrared Spectroscopy Authors: Cameron, A.D. / Smerdon, S.J. / Wilkinson, A.J. / Habash, J. / Helliwell, J.R. / Li, T. / Olson, J.S. #2: Journal: Biochemistry / Year: 1992 Title: High Resolution X-Ray Structures of Pig Metmyoglobin and Two Cd3 Mutants Mb(Lys45-->Arg) and Mb(Lys45-->Ser) Authors: Oldfield, T.J. / Smerdon, S.J. / Dauter, Z. / Petratos, K. / Wilson, K.S. / Wilkinson, A.J. #3: Journal: Acta Crystallogr.,Sect.B / Year: 1990 Title: Determination of the Crystal Structure of Recombinant Pig Myoglobin by Molecular Replacement and its Refinement Authors: Smerdon, S.J. / Oldfield, T.J. / Dodson, E.J. / Dodson, G.G. / Hubbard, R.E. / Wilkinson, A.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mni.cif.gz | 78.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mni.ent.gz | 60.3 KB | Display | PDB format |
PDBx/mmJSON format | 1mni.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mn/1mni ftp://data.pdbj.org/pub/pdb/validation_reports/mn/1mni | 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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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.995098, 0.0441, 0.08851), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX CHAIN RESIDUES CHAIN RESIDUES RMSD M1 A 1 - A 153 B 1 - B 153 0.537 | |
-Components
#1: Protein | Mass: 16983.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P02189 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.57 Å3/Da / Density % sol: 65.54 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 15 ℃ / pH: 7.1 / Method: vapor diffusion, hanging drop / Details: Dodson, G.(1988). Protein. Eng., 2, 233-237. | ||||||||||||||||||||
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 Highest resolution: 2.07 Å / Num. obs: 26337 / % possible obs: 88.6 % / Rmerge(I) obs: 0.042 |
Reflection shell | *PLUS Highest resolution: 2.07 Å / Lowest resolution: 2.11 Å / Rmerge(I) obs: 0.211 |
-Processing
Software |
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Refinement | Resolution: 2.07→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2.07→10 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor Rfree: 0.227 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |