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- PDB-2xin: PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLAN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xin | ||||||
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Title | PROTEIN ENGINEERING OF XYLOSE (GLUCOSE) ISOMERASE FROM ACTINOPLANES MISSOURIENSIS. 1. CRYSTALLOGRAPHY AND SITE-DIRECTED MUTAGENESIS OF METAL BINDING SITES | ||||||
![]() | D-XYLOSE ISOMERASE | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() xylose isomerase / D-xylose metabolic process / xylose isomerase activity / magnesium ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Janin, J. | ||||||
![]() | ![]() Title: Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 1. Crystallography and site-directed mutagenesis of metal binding sites. Authors: Jenkins, J. / Janin, J. / Rey, F. / Chiadmi, M. / van Tilbeurgh, H. / Lasters, I. / De Maeyer, M. / Van Belle, D. / Wodak, S.J. / Lauwereys, M. / Stanssens, P. / Matthyssens, G. / Lambeir, A.M. #1: ![]() Title: Protein Engineering of Xylose (Glucose) Isomerase from Actinoplanes Missouriensis. 2. Site-Directed Mutagenesis of the Xylose Binding Site Authors: Lambeir, A.-M. / Lauwereys, M. / Stanssens, P. / Mrabet, N.T. / Snauwaert, J. / Vantilbeurgh, H. / Matthyssens, G. / Lasters, I. / Demaeyer, M. / Wodak, S.J. / Jenkins, J. / Chiadmi, M. / Janin, J. #2: ![]() Title: Protein Engineering of Xylose (Glucose) Isomerase from Actinoplanes Missouriensis. 3. Changing Metal Specificity and the Ph Profile by Site-Directed Mutagenesis Authors: Vantilbeurgh, H. / Jenkins, J. / Chiadmi, M. / Wodak, J.Janin S.J. / Mrabet, N.T. / Lambeir, A.-M. #3: ![]() Title: Arginine Residues as Stabilizing Elements in Proteins Authors: Mrabet, N.T. / Van Denbroek, A. / Van Den Brande, I. / Stanssens, P. / Laroche, Y. / Lambeir, A.-M. / Matthijssens, G. / Jenkins, J. / Chiadmi, M. / Vantilbeurgh, H. / Rey, F. / Janin, J. / ...Authors: Mrabet, N.T. / Van Denbroek, A. / Van Den Brande, I. / Stanssens, P. / Laroche, Y. / Lambeir, A.-M. / Matthijssens, G. / Jenkins, J. / Chiadmi, M. / Vantilbeurgh, H. / Rey, F. / Janin, J. / Quax, W.J. / Lasters, I. / Demaeyer, M. / Wodak, S.J. #4: ![]() Title: Structural Analysis of the 2.8 Angstroms Model of Xylose Isomerase from Actinoplanes Missouriensis Authors: Rey, F. / Jenkins, J. / Janin, J. / Lasters, I. / Alard, P. / Claessens, M. / Matthyssens, G. / Wodak, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 328.1 KB | Display | ![]() |
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PDB format | ![]() | 266.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408 KB | Display | ![]() |
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Full document | ![]() | 447.6 KB | Display | |
Data in XML | ![]() | 35.4 KB | Display | |
Data in CIF | ![]() | 57.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1xinC ![]() 3xinC ![]() 4ximC ![]() 5ximC ![]() 5xinC ![]() 6ximC ![]() 7ximC ![]() 8ximC ![]() 9ximC C: citing same article ( |
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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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Atom site foot note | 1: RESIDUES PRO A 187, PRO B 187, PRO C 187, AND PRO D 187 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 43397.469 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Sugar | ChemComp-SOR / #3: Chemical | ChemComp-CO / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.96 Å3/Da / Density % sol: 68.93 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / pH: 6.8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 98930 / Num. measured all: 239000 / Rmerge(I) obs: 0.058 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Highest resolution: 2.3 Å /
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Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.3 Å / Num. reflection obs: 97899 / Rfactor obs: 0.154 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 21.2 Å2 |