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- PDB-1fzt: SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC EN... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fzt | ||||||
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Title | SOLUTION STRUCTURE AND DYNAMICS OF AN OPEN B-SHEET, GLYCOLYTIC ENZYME-MONOMERIC 23.7 KDA PHOSPHOGLYCERATE MUTASE FROM SCHIZOSACCHAROMYCES POMBE | ||||||
![]() | PHOSPHOGLYCERATE MUTASE | ||||||
![]() | ISOMERASE / open B-sheet-helices | ||||||
Function / homology | ![]() Glycolysis / Gluconeogenesis / Neutrophil degranulation / phosphoglycerate mutase activity / 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity / phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) / canonical glycolysis / gluconeogenesis / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
![]() | Uhrinova, S. / Uhrin, D. / Nairn, J. / Price, N.C. / Fothergill-Gilmore, L.A. | ||||||
![]() | ![]() Title: Solution structure and dynamics of an open beta-sheet, glycolytic enzyme, monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces pombe. Authors: Uhrinova, S. / Uhrin, D. / Nairn, J. / Price, N.C. / Fothergill-Gilmore, L.A. / Barlow, P.N. #1: ![]() Title: Backbone Assignment of Double Labelled 23.7 kDa Phosphoglycerate Mutase from Scizosaccharomyces pombe Authors: Uhrinova, S. / Uhrin, D. / Nairn, J. / Price, N.C. / Fothergill-Gilmore, L.A. / BARLOW, P.N. #2: ![]() Title: 3D HCCH3-TOCSY for Resonance Assignment of Methyl-containing Side Chains in (13)C-labeled Proteins Authors: Uhrin, D. / Uhrinova, S. / Leadbeater, C. / Nairn, J. / Price, N.C. / BARLOW, P.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 345.4 KB | Display | ![]() |
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Full document | ![]() | 698.8 KB | Display | |
Data in XML | ![]() | 140.2 KB | Display | |
Data in CIF | ![]() | 184.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 23800.139 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PMA91 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1mM phosphoglycerate mutase; 200mM sodium acetate, 200mM ammonium sulphate; 90% H2O, 10% D2O. Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.4 / Pressure: ambient / Temperature: 310 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: structures are based om 3125 noe restraints, 74 hydrogen bonds, and 149 torsion angles | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 55 / Conformers submitted total number: 21 |