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Yorodumi- PDB-1cgv: SITE DIRECTED MUTATIONS OF THE ACTIVE SITE RESIDUE TYROSINE 195 O... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cgv | |||||||||
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Title | SITE DIRECTED MUTATIONS OF THE ACTIVE SITE RESIDUE TYROSINE 195 OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 AFFECTING ACTIVITY AND PRODUCT SPECIFICITY | |||||||||
Components | CYCLOMALTODEXTRIN GLUCANOTRANSFERASE | |||||||||
Keywords | GLYCOSYLTRANSFERASE | |||||||||
Function / homology | Function and homology information cyclomaltodextrin glucanotransferase / cyclomaltodextrin glucanotransferase activity / starch binding / alpha-amylase activity / carbohydrate metabolic process / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | Bacillus circulans (bacteria) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | |||||||||
Authors | Strokopytov, B.V. / Dijkstra, B.W. | |||||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity. Authors: Penninga, D. / Strokopytov, B. / Rozeboom, H.J. / Lawson, C.L. / Dijkstra, B.W. / Bergsma, J. / Dijkhuizen, L. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Nucleotide Sequence and X-Ray Structure of Cyclodextrin Glycosyltransferase from Bacillus Circulans Strain 251 in a Maltose-Dependent Crystal Form Authors: Lawson, C.L.L. / Van Montfort, R. / Strokopytov, B. / Rozeboom, H.J. / Kalk, K.H. / De Vries, G.E. / Penninga, D. / Dijkhuizen, L. / Dijkstra, B.W. #2: Journal: J.Mol.Biol. / Year: 1990 Title: Maltodextrin-Dependent Crystallization of Cyclomaltodextrin Glucanotransferase from Bacillus Circulans Authors: Lawson, C.L.L. / Bergsma, J. / Bruinenberg, P.M. / De Vries, G.E. / Dijkhuizen, L. / Dijkstra, B.W. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cgv.cif.gz | 149.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cgv.ent.gz | 115.7 KB | Display | PDB format |
PDBx/mmJSON format | 1cgv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cgv_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 1cgv_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 1cgv_validation.xml.gz | 31 KB | Display | |
Data in CIF | 1cgv_validation.cif.gz | 42.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cg/1cgv ftp://data.pdbj.org/pub/pdb/validation_reports/cg/1cgv | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 372 / 2: CIS PROLINE - PRO 506 / 3: CIS PROLINE - PRO 624 / 4: CIS PROLINE - PRO 634 |
-Components
#1: Protein | Mass: 74559.484 Da / Num. of mol.: 1 / Mutation: Y195F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus circulans (bacteria) References: UniProt: P43379, cyclomaltodextrin glucanotransferase | ||||||
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#2: Polysaccharide | #3: Chemical | #4: Water | ChemComp-HOH / | Has protein modification | Y | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.84 % |
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Crystal grow | *PLUS Method: vapor diffusion |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 29 Å / Num. obs: 28296 / % possible obs: 87.3 % / Num. measured all: 84161 / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 2.58 Å / % possible obs: 45 % |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||
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Refinement | Resolution: 2.5→20 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refinement | *PLUS Highest resolution: 2.5 Å | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 25.3 Å2 | ||||||||||||||||||||||||
Refine LS restraints | *PLUS
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