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- PDB-1xie: MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-X... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xie | ||||||
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Title | MODES OF BINDING SUBSTRATES AND THEIR ANALOGUES TO THE ENZYME D-XYLOSE ISOMERASE | ||||||
![]() | D-XYLOSE ISOMERASE | ||||||
![]() | ISOMERASE(INTRAMOLECULAR OXIDOREDUCTASE) | ||||||
Function / homology | ![]() xylose isomerase / D-xylose metabolic process / xylose isomerase activity / magnesium ion binding / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Carrell, H.L. / Glusker, J.P. | ||||||
![]() | ![]() Title: Modes of binding substrates and their analogues to the enzyme D-xylose isomerase. Authors: Carrell, H.L. / Hoier, H. / Glusker, J.P. #1: ![]() Title: X-Ray Analysis of D-Xylose Isomerase at 1.9 Angstroms: Native Enzyme in Complex with Substrate and with a Mechanism-Designed Inactivator Authors: Carrell, H.L. / Glusker, J.P. / Burger, V. / Manfre, F. / Biellmann, D.Tritsch J.-F. #2: ![]() Title: Comparison of Backbone Structures of Glucose Isomerase from Streptomyces and Arthrobacter Authors: Henrick, K. / Blow, D.M. / Carrell, H.L. / Glusker, J.P. #3: ![]() Title: X-Ray Crystal Structure of D-Xylose Isomerase at 4-Angstroms Resolution Authors: Carrell, H.L. / Rubin, B.H. / Hurley, T.J. / Glusker, J.P. | ||||||
History |
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Remark 700 | SHEET THE STRUCTURE OF THE MONOMER IS AN EIGHT-FOLD ALPHA-BETA BARREL WITH AN EXTENDED C-TERMINAL ...SHEET THE STRUCTURE OF THE MONOMER IS AN EIGHT-FOLD ALPHA-BETA BARREL WITH AN EXTENDED C-TERMINAL LOOP WHICH FACILITATES AGGREGATION OF MONOMERS TO TETRAMERS. TETRAMERS ARE POSITIONED ON THE 222 SYMMETRY SITE AT THE ORIGIN OF THE CELL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.1 KB | Display | ![]() |
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PDB format | ![]() | 74 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1xibC ![]() 1xicC ![]() 1xidC ![]() 1xifC ![]() 1xigC ![]() 1xihC ![]() 1xiiC ![]() 1xijC 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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1 | ![]()
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Unit cell |
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Atom site foot note | 1: ASN 2 - TYR 3 OMEGA =215.61 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: CIS PROLINE - PRO 187 3: ALA 386 - ARG 387 OMEGA =276.83 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||||||
Components on special symmetry positions |
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Components
#1: Protein | Mass: 43254.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||
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#2: Sugar | ChemComp-ASO / | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.76 Å3/Da / Density % sol: 55.5 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 1.7→10 Å / σ(I): 1.5 /
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Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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