Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. Determined by X-ray diffraction at 2.24 Å resolution. Released 15 May 2013.
Explore 4J15 in 3D Show helices and sheets RCSB PDB PDBe
4J15 contains 53 α-helices and 46 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-28 | 3 | |
| β-strand | 29-31 | 3 | 1 |
| α-helix | 32-34 | 3 | |
| β-strand | 45 | 1 | 1 |
| α-helix | 46-47 | 2 | |
| α-helix | 48-50 | 3 | |
| α-helix | 53-55 | 3 | |
| β-strand | 59-72 | 14 | 1 |
| β-strand | 75-82 | 8 | 1 |
| β-strand | 85-92 | 8 | 1 |
| β-strand | 93 | 1 | 2 |
| β-strand | 97 | 1 | 2 |
| α-helix | 99-107 | 9 | |
| α-helix | 109 | 1 | |
| β-strand | 113-122 | 10 | 1 |
| β-strand | 135-146 | 12 | 1 |
| α-helix | 147-149 | 3 | |
| α-helix | 156-160 | 5 | |
| α-helix | 176-181 | 6 | |
| α-helix | 183-186 | 4 | |
| α-helix | 190-212 | 23 | |
| β-strand | 216-217 | 2 | 3 |
| α-helix | 250-259 | 10 | |
| β-strand | 264-271 | 8 | 3 |
| β-strand | 286-294 | 9 | 3 |
| α-helix | 300-320 | 21 | |
| α-helix | 322-331 | 10 | |
| α-helix | 335-337 | 3 | |
| β-strand | 344-347 | 4 | 3 |
| α-helix | 348-357 | 10 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-384 | 15 | |
| β-strand | 388-392 | 5 | 3 |
| β-strand | 395 | 1 | 4 |
| α-helix | 396-398 | 3 | |
| β-strand | 403 | 1 | 5 |
| α-helix | 404 | 1 | |
| β-strand | 405 | 1 | 6 |
| α-helix | 406 | 1 | |
| β-strand | 412 | 1 | 4 |
| β-strand | 413 | 1 | 6 |
| β-strand | 415-420 | 6 | 3 |
| β-strand | 423-430 | 8 | 3 |
| β-strand | 431 | 1 | 5 |
| α-helix | 435-444 | 10 | |
| α-helix | 450-452 | 3 | |
| α-helix | 453-457 | 5 | |
| β-strand | 466-472 | 7 | 3 |
| α-helix | 473-481 | 9 | |
| α-helix | 486-489 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 26-28 | 3 | |
| β-strand | 29-31 | 3 | 7 |
| α-helix | 32-34 | 3 | |
| β-strand | 45 | 1 | 7 |
| α-helix | 46-47 | 2 | |
| α-helix | 48-50 | 3 | |
| α-helix | 53-55 | 3 | |
| β-strand | 59-72 | 14 | 7 |
| β-strand | 75-82 | 8 | 7 |
| β-strand | 85-92 | 8 | 7 |
| β-strand | 93 | 1 | 8 |
| β-strand | 97 | 1 | 8 |
| α-helix | 99-107 | 9 | |
| α-helix | 108-109 | 2 | |
| β-strand | 113-122 | 10 | 7 |
| β-strand | 135-146 | 12 | 7 |
| α-helix | 147-149 | 3 | |
| α-helix | 156-159 | 4 | |
| α-helix | 176-181 | 6 | |
| α-helix | 183-186 | 4 | |
| α-helix | 190-212 | 23 | |
| β-strand | 216-217 | 2 | 9 |
| α-helix | 250-259 | 10 | |
| β-strand | 264-271 | 8 | 9 |
| β-strand | 286-294 | 9 | 9 |
| α-helix | 300-320 | 21 | |
| α-helix | 322-331 | 10 | |
| α-helix | 335-337 | 3 | |
| β-strand | 344-347 | 4 | 9 |
| α-helix | 348-357 | 10 | |
| α-helix | 366-369 | 4 | |
| α-helix | 370-384 | 15 | |
| β-strand | 388-392 | 5 | 9 |
| β-strand | 395 | 1 | 10 |
| α-helix | 396-398 | 3 | |
| β-strand | 403 | 1 | 11 |
| α-helix | 404 | 1 | |
| β-strand | 405 | 1 | 12 |
| α-helix | 406 | 1 | |
| β-strand | 412 | 1 | 10 |
| β-strand | 413 | 1 | 12 |
| β-strand | 415-420 | 6 | 9 |
| β-strand | 423-430 | 8 | 9 |
| β-strand | 431 | 1 | 11 |
| α-helix | 435-444 | 10 | |
| α-helix | 453-457 | 5 | |
| β-strand | 466-472 | 7 | 9 |
| α-helix | 473-480 | 8 | |
| α-helix | 486-489 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aspartate--tRNA ligase, cytoplasmic | A, B | protein | 521 | Homo sapiens | P14868 (AlphaFold model) |
>4J15_1 Aspartate--tRNA ligase, cytoplasmic (chains A, B) MGSSHHHHHHSSGLVPRGSHMPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEK PDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQ MVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAV RPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQT PKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTH RHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFL EPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRP FYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFR FGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP
Crystal structure of human cytosolic aspartyl-tRNA synthetase, a component of multi-tRNA synthetase complex. Kim, K.R., Park, S.H., Kim, H.S. et al. Proteins (2013) 81:1840-1846. DOI 10.1002/prot.24306 · PubMed
Other PDB entries of the same protein (UniProt P14868 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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