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Open data
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Basic information
Entry | Database: PDB / ID: 4ah6 | ||||||
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Title | Human mitochondrial aspartyl-tRNA synthetase | ||||||
![]() | ASPARTATE--TRNA LIGASE, MITOCHONDRIAL | ||||||
![]() | LIGASE | ||||||
Function / homology | ![]() mitochondrial asparaginyl-tRNA aminoacylation / aspartate-tRNA(Asn) ligase activity / aspartate-tRNA ligase / aspartate-tRNA ligase activity / tRNA aminoacylation / Mitochondrial tRNA aminoacylation / tRNA aminoacylation for protein translation / tRNA binding / mitochondrial matrix / protein homodimerization activity ...mitochondrial asparaginyl-tRNA aminoacylation / aspartate-tRNA(Asn) ligase activity / aspartate-tRNA ligase / aspartate-tRNA ligase activity / tRNA aminoacylation / Mitochondrial tRNA aminoacylation / tRNA aminoacylation for protein translation / tRNA binding / mitochondrial matrix / protein homodimerization activity / mitochondrion / nucleoplasm / ATP binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Neuenfeldt, A. / Sissler, M. / Lorber, B. / Florentz, C. / Sauter, C. | ||||||
![]() | ![]() Title: Thermodynamic Properties Distinguish Human Mitochondrial Aspartyl-tRNA Synthetase from Bacterial Homolog with Same 3D Architecture Authors: Ennifar, E. / Florentz, C. / Gaudry, A. / Lorber, B. / Neuenfeldt, A. / Sauter, C. / Sissler, M. #1: Journal: Biochimie / Year: 2009 Title: Peculiar Inhibition of Human Mitochondrial Aspartyl-tRNA Synthetase by Adenylate Analogs. Authors: Messmer, M. / Blais, S.P. / Balg, C. / Chenevert, R. / Grenier, L. / Lague, P. / Sauter, C. / Sissler, M. / Giege, R. / Lapointe, J. / Florentz, C. #2: Journal: J.Biol.Chem. / Year: 2006 Title: Loss of a Primordial Identity Element for a Mammalian Mitochondrial Aminoacylation System. Authors: Fender, A. / Sauter, C. / Messmer, M. / Putz, J. / Giege, R. / Florentz, C. / Sissler, M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "DA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 467.7 KB | Display | ![]() |
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PDB format | ![]() | 386.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.7 KB | Display | ![]() |
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Full document | ![]() | 535.7 KB | Display | |
Data in XML | ![]() | 86.9 KB | Display | |
Data in CIF | ![]() | 114.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1c0aS S: Starting model for refinement |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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