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Yorodumi- PDB-3pgk: The structure of yeast phosphoglycerate kinase at 0.25 nm resolution -
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Open data
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Basic information
| Entry | Database: PDB / ID: 3pgk | |||||||||
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| Title | The structure of yeast phosphoglycerate kinase at 0.25 nm resolution | |||||||||
Components | PHOSPHOGLYCERATE KINASE | |||||||||
Keywords | TRANSFERASE / PHOSPHOTRANSFERASE(CARBOXYL AS ACCEPTOR) | |||||||||
| Function / homology | Function and homology informationGluconeogenesis / Glycolysis / phosphoglycerate kinase / phosphoglycerate kinase activity / glycolytic process / gluconeogenesis / ADP binding / mitochondrion / ATP binding / metal ion binding ...Gluconeogenesis / Glycolysis / phosphoglycerate kinase / phosphoglycerate kinase activity / glycolytic process / gluconeogenesis / ADP binding / mitochondrion / ATP binding / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | |||||||||
Authors | Shaw, P.J. / Walker, N.P. / Watson, H.C. | |||||||||
Citation | Journal: Embo J. / Year: 1982Title: Sequence and structure of yeast phosphoglycerate kinase. Authors: Watson, H.C. / Walker, N.P. / Shaw, P.J. / Bryant, T.N. / Wendell, P.L. / Fothergill, L.A. / Perkins, R.E. / Conroy, S.C. / Dobson, M.J. / Tuite, M.F. #1: Journal: Biochem.J. / Year: 1983Title: The Complete Amino Acid Sequence of Yeast Phosphoglycerate Kinase Authors: Perkins, R.E. / Conroy, S.C. / Dunbar, B. / Fothergill, L.A. / Tuite, M.F. / Dobson, M.J. / Kingsman, S.M. / Kingsman, A.J. #2: Journal: Embo J. / Year: 1982Title: Sequence and Structure of Yeast Phosphoglycerate Kinase Authors: Watson, H.C. / Walker, N.P.C. / Shaw, P.J. / Bryant, T.N. / Wendell, P.L. / Fothergill, L.A. / Perkins, R.E. / Conroy, S.C. / Dobson, M.J. / Tuite, M.F. / Kingsman, A.J. / Kingsman, S.M. #3: Journal: Nature / Year: 1974Title: Structure of Yeast Phosphoglycerate Kinase Authors: Bryant, T.N. / Watson, H.C. / Wendell, P.L. #4: Journal: Nature New Biol. / Year: 1972Title: Low Resolution Structure of Yeast Phosphoglycerate Kinase Authors: Wendell, P.L. / Bryant, T.N. / Watson, H.C. #5: Journal: J.Mol.Biol. / Year: 1971Title: Crystallographic Study of Yeast Phosphoglycerate Kinase Authors: Watson, H.C. / Wendell, P.L. / Scopes, R.K. | |||||||||
| History |
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| Remark 700 | SHEET CAUTION. THE DEFINITION OF THE BEGINNING AND END OF HELICES AND SHEET STRANDS GIVEN BELOW ...SHEET CAUTION. THE DEFINITION OF THE BEGINNING AND END OF HELICES AND SHEET STRANDS GIVEN BELOW DEPENDS SOMEWHAT ON THE CRITERIA USED TO DEFINE A *GOOD* HYDROGEN BOND. TURNS LISTED BELOW ARE THOSE WHERE CA(1)-CA(4) IS LESS THAN 5.7 ANGSTROMS AND O(1)-N(4) IS LESS THAN 3.2 ANGSTROMS. FULL TURN DEFINITION MUST AWAIT FURTHER REFINEMENT. |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 3pgk.cif.gz | 100.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb3pgk.ent.gz | 58.8 KB | Display | PDB format |
| PDBx/mmJSON format | 3pgk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 3pgk_validation.pdf.gz | 476.6 KB | Display | wwPDB validaton report |
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| Full document | 3pgk_full_validation.pdf.gz | 721 KB | Display | |
| Data in XML | 3pgk_validation.xml.gz | 54.9 KB | Display | |
| Data in CIF | 3pgk_validation.cif.gz | 69.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pg/3pgk ftp://data.pdbj.org/pub/pdb/validation_reports/pg/3pgk | HTTPS FTP |
-Related structure data
| 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: THIS ATOM MAY BE MAGNESIUM OR MANGANESE. |
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Components
| #1: Protein | Mass: 44652.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P00560, phosphoglycerate kinase |
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| #2: Chemical | ChemComp-MG / |
| #3: Chemical | ChemComp-ATP / |
| #4: Chemical | ChemComp-3PG / |
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 51.97 % |
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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
| Refinement | Highest resolution: 2.5 Å | ||||||||||||
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| Refinement step | Cycle: LAST / Highest resolution: 2.5 Å
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