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- PDB-1o7d: The structure of the bovine lysosomal a-mannosidase suggests a no... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o7d | ||||||||||||
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Title | The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation | ||||||||||||
![]() | (Lysosomal alpha- ...) x 5 | ||||||||||||
![]() | HYDROLASE / GLYCOSYL HYDROLASE FAMILY 38 / A-MANNOSIDASE / LYSOSOMAL | ||||||||||||
Function / homology | ![]() Lysosomal oligosaccharide catabolism / alpha-mannosidase / alpha-mannosidase activity / mannose metabolic process / vacuolar membrane / Neutrophil degranulation / carbohydrate binding / learning or memory / lysosome / zinc ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Heikinheimo, P. / Helland, R. / Leiros, H.S. / Leiros, I. / Karlsen, S. / Evjen, G. / Ravelli, R. / Schoehn, G. / Ruigrok, R. / Tollersrud, O.-K. ...Heikinheimo, P. / Helland, R. / Leiros, H.S. / Leiros, I. / Karlsen, S. / Evjen, G. / Ravelli, R. / Schoehn, G. / Ruigrok, R. / Tollersrud, O.-K. / Mcsweeney, S. / Hough, E. | ||||||||||||
![]() | ![]() Title: The Structure of Bovine Lysosomal Alpha-Mannosidase Suggests a Novel Mechanism for Low-Ph Activation Authors: Heikinheimo, P. / Helland, R. / Leiros, H.S. / Leiros, I. / Karlsen, S. / Evjen, G. / Ravelli, R. / Schoehn, G. / Ruigrok, R. / Tollersrud, O.-K. / Mcsweeney, S. / Hough, E. #1: Journal: Eur.J.Biochem. / Year: 1997 Title: Purification of Bovine Lysosomal A-Mannosidase, Characterization of its Gene and Determination of Two Mutations that Cause A- Mannosidosis Authors: Tollersrud, O.-K. / Berg, T. / Healy, P. / Evjen, G. / Ramachandran, U. | ||||||||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 187.6 KB | Display | ![]() |
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PDB format | ![]() | 145.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 31.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1htyS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | THE MOLECULE IS A DIMER IN SOLUTION, BUT THE CURRENTENTRY DESCRIBES A MONONER IN THE ASYMMETRIC UNIT THATIS FORMED OF CHAINS A-E RESULTING FROM PROTEOLYTICPROCESSING OF A SINGLE GENE PRODUCT, AND HENCECLASSIFIED AS A PENTAMER |
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Components
-Lysosomal alpha- ... , 5 types, 5 molecules ABCDE
#1: Protein | Mass: 34527.223 Da / Num. of mol.: 1 / Fragment: ALPHA-MANNOSIDASE A PEPTIDE, RESIDUES 51-347 / Source method: isolated from a natural source / Details: GLYCOSYLATED / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 9649.912 Da / Num. of mol.: 1 / Fragment: ALPHA-MANNOSIDASE B PEPTIDE, RESIDUES 348-431 / Source method: isolated from a natural source / Details: GLYCOSYLATED / Source: (natural) ![]() ![]() |
#3: Protein | Mass: 17596.104 Da / Num. of mol.: 1 / Fragment: ALPHA-MANNOSIDASE C PEPTIDE, RESIDUES 432-590 / Source method: isolated from a natural source / Details: GLYCOSYLATED / Source: (natural) ![]() ![]() |
#4: Protein | Mass: 32225.463 Da / Num. of mol.: 1 / Fragment: ALPHA-MANNOSIDASE D PEPTIDE, RESIDUES 592-873 / Source method: isolated from a natural source / Details: GLYCOSYLATED / Source: (natural) ![]() ![]() |
#5: Protein | Mass: 14054.821 Da / Num. of mol.: 1 / Fragment: ALPHA-MANNOSIDASE E PEPTIDE, RESIDUES 874-999 / Source method: isolated from a natural source / Details: GLYCOSYLATED / Source: (natural) ![]() ![]() |
-Sugars , 3 types, 5 molecules ![](data/chem/img/NAG.gif)
#6: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||
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#7: Polysaccharide | Source method: isolated from a genetically manipulated source #8: Sugar | ChemComp-NAG / | |
-Non-polymers , 4 types, 43 molecules ![](data/chem/img/TRS.gif)
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![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/HOH.gif)
#9: Chemical | ChemComp-TRS / | ||
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#10: Chemical | ChemComp-ZN / | ||
#11: Chemical | #12: Water | ChemComp-HOH / | |
-Details
Compound details | ESSENTIAL IN THE CATABOLISM OF N-LINKED CARBOHYDRATES DURING GLYCOPROTEIN TURNOVER. HYDROLYSES ...ESSENTIAL IN THE CATABOLISM |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | pH: 7.5 Details: PROTEIN 9 MG/ML IN 20 MM TRIS-CL, PH 7.5, 150 MM NACL MIXED 1:1 WITH 100 MM TRIS-CL, PH 7.5, 50 % SAT. (NH4)2SO4 | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-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: 0.9395 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. obs: 60071 / % possible obs: 89 % / Redundancy: 3 % / Biso Wilson estimate: 51.3 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 15.9 |
Reflection shell | Resolution: 2.7→2.76 Å / Rmerge(I) obs: 0.54 / Mean I/σ(I) obs: 2.1 / % possible all: 78 |
Reflection | *PLUS Lowest resolution: 30 Å / % possible obs: 89.4 % |
Reflection shell | *PLUS % possible obs: 77.7 % / Redundancy: 3 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HTY Resolution: 2.7→30 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 3231490 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 32.9541 Å2 / ksol: 0.32892 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 38.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.7→30 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.87 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 30 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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