+Open data
-Basic information
Entry | Database: PDB / ID: 1jda | ||||||
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Title | MALTOTETRAOSE-FORMING EXO-AMYLASE | ||||||
Components | 1,4-ALPHA MALTOTETRAHYDROLASE | ||||||
Keywords | HYDROLASE / MALTOTETRAOSE-FORMING EXO AMYLASE | ||||||
Function / homology | Function and homology information glucan 1,4-alpha-maltotetraohydrolase / glucan 1,4-alpha-maltotetraohydrolase activity / starch catabolic process / starch binding / alpha-amylase activity / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | Pseudomonas stutzeri (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Yoshioka, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1997 Title: Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose. Authors: Yoshioka, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. #1: Journal: J.Mol.Biol. / Year: 1997 Title: Crystal Structure of a Maltotetraose-Forming Exo-Amylase from Pseudomonas Stutzeri Authors: Morishita, Y. / Hasegawa, K. / Matsuura, Y. / Katsube, Y. / Kubota, M. / Sakai, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jda.cif.gz | 96.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jda.ent.gz | 76.7 KB | Display | PDB format |
PDBx/mmJSON format | 1jda.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jda_validation.pdf.gz | 392 KB | Display | wwPDB validaton report |
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Full document | 1jda_full_validation.pdf.gz | 418.2 KB | Display | |
Data in XML | 1jda_validation.xml.gz | 13.8 KB | Display | |
Data in CIF | 1jda_validation.cif.gz | 20.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jd/1jda ftp://data.pdbj.org/pub/pdb/validation_reports/jd/1jda | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 47408.637 Da / Num. of mol.: 1 / Mutation: E219Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas stutzeri (bacteria) / Strain: MO-19 / Production host: Escherichia coli (E. coli) / Strain (production host): HB101 References: UniProt: P13507, glucan 1,4-alpha-maltotetraohydrolase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 57 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Dec 3, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 17893 / % possible obs: 65.8 % / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.105 |
Reflection | *PLUS Highest resolution: 2.2 Å / Num. measured all: 39300 |
-Processing
Software |
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Refinement | Resolution: 2.2→10 Å / σ(F): 2 / Details: X-PLOR WAS ALSO USED. /
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROFFT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.174 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |