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Yorodumi- PDB-1mea: METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND H... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mea | ||||||
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Title | METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS | ||||||
Components | METHIONYL-tRNA SYNTHETASEMethionine—tRNA ligase | ||||||
Keywords | AMINOACYL-TRNA SYNTHASE | ||||||
Function / homology | Function and homology information 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 | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Fourmy, D. / Dardel, F. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1993 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: Journal: J.Mol.Biol. / Year: 1993 Title: Mapping of the Zinc Binding Domain of Escherichia Coli Methionyl-tRNA Synthetase Authors: Fourmy, D. / Meinnel, T. / Mechulam, Y. / Blanquet, S. #2: Journal: J.Mol.Biol. / Year: 1990 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mea.cif.gz | 17 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mea.ent.gz | 9.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mea.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/me/1mea ftp://data.pdbj.org/pub/pdb/validation_reports/me/1mea | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Atom site foot note | 1: CYS 10 - PRO 11 OMEGA ANGLE = 216.960 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: SER 15 - PRO 16 OMEGA ANGLE = 216.723 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.) Escherichia coli (E. coli) / Gene: GAG / Gene (production host): GAG / References: UniProt: P00959, methionine-tRNA ligase |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Processing
Software |
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NMR ensemble | Conformers submitted total number: 1 |