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- PDB-1cdg: NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cdg | |||||||||
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Title | NUCLEOTIDE SEQUENCE AND X-RAY STRUCTURE OF CYCLODEXTRIN GLYCOSYLTRANSFERASE FROM BACILLUS CIRCULANS STRAIN 251 IN A MALTOSE-DEPENDENT CRYSTAL FORM | |||||||||
![]() | CYCLODEXTRIN GLYCOSYL-TRANSFERASE | |||||||||
![]() | TRANSFERASE(GLUCANOTRANSFERASE) | |||||||||
Function / homology | ![]() cyclomaltodextrin glucanotransferase / cyclomaltodextrin glucanotransferase activity / starch binding / alpha-amylase activity / carbohydrate metabolic process / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Lawson, C.L. / Van Montfort, R. / Strokopytov, B.V. / Kalk, K.H. / Rozeboom, H.J. / Dijkstra, B.W. | |||||||||
![]() | ![]() 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. / van Montfort, R. / Strokopytov, B. / Rozeboom, H.J. / Kalk, K.H. / de Vries, G.E. / Penninga, D. / Dijkhuizen, L. / Dijkstra, B.W. #1: ![]() Title: Maltodextrin-Dependent Crystallization of Cyclomaltodextrin Glucanotransferase from Bacillus Circulans Authors: Lawson, C.L. / Bergsma, J. / Bruinenberg, P.M. / De Vries, G. / Dijkhuizen, L. / Dijkstra, B.W. | |||||||||
History |
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Remark 650 | HELIX RESIDUES 54 - 62 AND 65 - 68 OF THE HELIX RECORD BELOW CONSTITUTE ONE HELIX. | |||||||||
Remark 700 | SHEET THE SHEET PRESENTED AS *AB8* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. ...SHEET THE SHEET PRESENTED AS *AB8* ON SHEET RECORDS BELOW IS ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 152.9 KB | Display | ![]() |
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PDB format | ![]() | 121.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 31 KB | Display | |
Data in CIF | ![]() | 46.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Atom site foot note | 1: RESIDUES PRO 372, PRO 506, PRO 624, AND PRO 634 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 74575.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P43379, cyclomaltodextrin glucanotransferase | ||||
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#2: Polysaccharide | #3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.97 Å3/Da / Density % sol: 58.62 % | ||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||
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 |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.164 / Highest resolution: 2 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Refinement | *PLUS σ(F): 0 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 24.3 Å2 | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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