Free aspartyl-tRNA synthetase (ASPRS) (e.c. 6.1.1.12) from yeast. Determined by X-ray diffraction at 2.3 Å resolution. Released 24 Sept 2000.
Explore 1EOV in 3D Show helices and sheets RCSB PDB PDBe
1EOV contains 27 α-helices and 25 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 75-77 | 3 | 1 |
| α-helix | 78-80 | 3 | |
| α-helix | 85-87 | 3 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-98 | 3 | |
| β-strand | 108-120 | 13 | 1 |
| β-strand | 125-132 | 8 | 1 |
| β-strand | 135-142 | 8 | 1 |
| α-helix | 151-157 | 7 | |
| α-helix | 160-161 | 2 | |
| β-strand | 165-174 | 10 | 1 |
| β-strand | 184-198 | 15 | 1 |
| α-helix | 208-211 | 4 | |
| α-helix | 215-220 | 6 | |
| α-helix | 223-225 | 3 | |
| α-helix | 228-233 | 6 | |
| α-helix | 235-238 | 4 | |
| α-helix | 242-264 | 23 | |
| β-strand | 268-269 | 2 | 2 |
| β-strand | 275-276 | 2 | 3 |
| β-strand | 288-291 | 4 | 3 |
| β-strand | 294-298 | 5 | 3 |
| α-helix | 303-311 | 9 | |
| β-strand | 316-324 | 9 | 2 |
| β-strand | 337-346 | 10 | 2 |
| α-helix | 352-372 | 21 | |
| α-helix | 374-383 | 10 | |
| α-helix | 396-397 | 2 | |
| β-strand | 398-401 | 4 | 2 |
| α-helix | 402-411 | 10 | |
| α-helix | 420-423 | 4 | |
| α-helix | 424-437 | 14 | |
| β-strand | 442-446 | 5 | 2 |
| β-strand | 449 | 1 | 4 |
| α-helix | 450-452 | 3 | |
| β-strand | 457 | 1 | 5 |
| α-helix | 458 | 1 | |
| β-strand | 459 | 1 | 6 |
| α-helix | 460 | 1 | |
| β-strand | 466 | 1 | 4 |
| β-strand | 467 | 1 | 6 |
| β-strand | 469-474 | 6 | 2 |
| β-strand | 477-484 | 8 | 2 |
| β-strand | 485 | 1 | 5 |
| α-helix | 486 | 1 | |
| α-helix | 489-498 | 10 | |
| α-helix | 509-515 | 7 | |
| β-strand | 522-528 | 7 | 2 |
| α-helix | 529-536 | 8 | |
| α-helix | 542-545 | 4 | |
| β-strand | 551 | 1 | 7 |
| β-strand | 554 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Aspartyl-tRNA synthetase | A | protein | 487 | Saccharomyces cerevisiae | P04802 (AlphaFold model) |
>1EOV_1 ASPARTYL-TRNA SYNTHETASE (chains A) AKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAFLTL RQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNLEIH ITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAIFRI QAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQQLI VADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFSELP KRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENEKFL GKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIHDHA LLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASLFPR DPKRLRP
The free yeast aspartyl-tRNA synthetase differs from the tRNA(Asp)-complexed enzyme by structural changes in the catalytic site, hinge region, and anticodon-binding domain. Sauter, C., Lorber, B., Cavarelli, J. et al. J Mol Biol (2000) 299:1313-1324. DOI 10.1006/jmbi.2000.3791 · PubMed
Other PDB entries of the same protein (UniProt P04802 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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