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- PDB-1med: METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND H... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1med | ||||||
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Title | METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS | ||||||
![]() | METHIONYL-tRNA SYNTHETASE | ||||||
![]() | AMINOACYL-TRNA SYNTHASE | ||||||
Function / homology | ![]() methionine-tRNA ligase / methionine-tRNA ligase activity / methionyl-tRNA aminoacylation / aminoacyl-tRNA synthetase multienzyme complex / tRNA binding / protein homodimerization activity / zinc ion binding / ATP binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Fourmy, D. / Dardel, F. | ||||||
![]() | ![]() Title: Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins. Authors: Fourmy, D. / Dardel, F. / Blanquet, S. #1: ![]() Title: Mapping of the Zinc Binding Domain of Escherichia Coli Methionyl-tRNA Synthetase Authors: Fourmy, D. / Meinnel, T. / Mechulam, Y. / Blanquet, S. #2: ![]() Title: Crystallographic Study at 2.5 Angstroms Resolution of the Interaction of Methionyl-tRNA Synthetase from Escherichia Coli with ATP Authors: Brunie, S. / Zelwer, C. / Risler, J.-L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 93 KB | Display | ![]() |
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PDB format | ![]() | 57.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 350.1 KB | Display | ![]() |
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Full document | ![]() | 416.5 KB | Display | |
Data in XML | ![]() | 8.3 KB | Display | |
Data in CIF | ![]() | 12.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Atom site foot note | 1: CYS 10 - PRO 11 MODEL 1 OMEGA =221.65 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: SER 15 - PRO 16 MODEL 1 OMEGA =230.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: CYS 10 - PRO 11 MODEL 2 OMEGA =226.31 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: SER 15 - PRO 16 MODEL 2 OMEGA =233.15 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 5: CYS 10 - PRO 11 MODEL 4 OMEGA =212.66 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 6: SER 15 - PRO 16 MODEL 4 OMEGA =223.41 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 7: CYS 10 - PRO 11 MODEL 5 OMEGA =227.82 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 8: CYS 10 - PRO 11 MODEL 6 OMEGA =216.14 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 9: SER 15 - PRO 16 MODEL 6 OMEGA =213.88 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 10: CYS 10 - PRO 11 MODEL 8 OMEGA =211.33 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 11: SER 15 - PRO 16 MODEL 8 OMEGA =214.66 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 12: CYS 10 - PRO 11 MODEL 9 OMEGA =215.05 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 13: SER 15 - PRO 16 MODEL 9 OMEGA =234.13 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 14: CYS 10 - PRO 11 MODEL 10 OMEGA =221.52 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 15: SER 15 - PRO 16 MODEL 10 OMEGA =220.78 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 16: CYS 10 - PRO 11 MODEL 11 OMEGA =212.67 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 17: SER 15 - PRO 16 MODEL 11 OMEGA =236.00 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | |||||||||
NMR ensembles |
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Components
#1: Protein/peptide | Mass: 2969.311 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Processing
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NMR ensemble | Conformers submitted total number: 11 |