2.2 Angstrom Crystal Structure of a Human Arginyl-tRNA Synthetase. Determined by X-ray diffraction at 2.22 Å resolution. Released 30 Mar 2016.
Explore 4ZAJ in 3D Show helices and sheets RCSB PDB PDBe
4ZAJ contains 33 α-helices and 20 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 |
|---|---|---|---|
| α-helix | 4-19 | 16 | |
| β-strand | 30-32 | 3 | 1 |
| β-strand | 41-43 | 3 | 1 |
| α-helix | 45-51 | 7 | |
| α-helix | 62-71 | 10 | |
| α-helix | 73-75 | 3 | |
| β-strand | 79-83 | 5 | 1 |
| β-strand | 90-94 | 5 | 1 |
| α-helix | 96-109 | 14 | |
| α-helix | 113-116 | 4 | |
| β-strand | 121-125 | 5 | 2 |
| α-helix | 129 | 1 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 137-155 | 19 | |
| β-strand | 159-164 | 6 | 2 |
| β-strand | 167 | 1 | 3 |
| α-helix | 172-183 | 12 | |
| α-helix | 185-188 | 4 | |
| α-helix | 197-210 | 14 | |
| α-helix | 213-226 | 14 | |
| α-helix | 233-253 | 21 | |
| β-strand | 259-260 | 2 | 2 |
| α-helix | 263-269 | 7 | |
| α-helix | 270-279 | 10 | |
| β-strand | 284-286 | 3 | 4 |
| β-strand | 289-292 | 4 | 4 |
| α-helix | 300 | 1 | |
| β-strand | 301-304 | 4 | 4 |
| β-strand | 310 | 1 | 4 |
| α-helix | 312-325 | 14 | |
| β-strand | 331-337 | 7 | 2 |
| α-helix | 338-340 | 3 | |
| α-helix | 341-353 | 13 | |
| β-strand | 363-369 | 7 | 2 |
| α-helix | 370-371 | 2 | |
| β-strand | 372-373 | 2 | 5 |
| β-strand | 379 | 1 | 5 |
| α-helix | 387-389 | 3 | |
| α-helix | 390-406 | 17 | |
| α-helix | 415-416 | 2 | |
| α-helix | 417-422 | 6 | |
| α-helix | 423-436 | 14 | |
| β-strand | 444-445 | 2 | 5 |
| α-helix | 448-451 | 4 | |
| α-helix | 459-474 | 16 | |
| α-helix | 480-489 | 10 | |
| α-helix | 497-506 | 10 | |
| α-helix | 509-519 | 11 | |
| α-helix | 523-542 | 20 | |
| β-strand | 546-548 | 3 | 6 |
| β-strand | 555-558 | 4 | 6 |
| α-helix | 560-580 | 21 | |
| α-helix | 582-584 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Arginine--tRNA ligase, cytoplasmic | A | protein | 601 | Homo sapiens | P54136 (AlphaFold model) |
>4ZAJ_1 Arginine--tRNA ligase, cytoplasmic (chains A) MINIISRLQEVFGHAIKAAYPDLENPPLLVTPSQQAKFGDYQCNSAMGISQMLKTKEQKV NPREIAENITKHLPDNECIEKVEIAGPGFINVHLRKDFVSEQLTSLLVNGVQLPALGENK KVIVDFSSPNIAKEMHVGHLRSTIIGESISRLFEFAGYDVLRLNHVGDWGTQFGMLIAHL QDKFPDYLTVSPPIGDLQVFYKESKKRFDTEEEFKKRAYQCVVLLQGKNPDITKAWKLIC DVSRQELNKIYDALDVSLIERGESFYQDRMNDIVKEFEDRGFVQVDDGRKIVFVPGCSIP LTIVKSDGGYTYDTSDLAAIKQRLFEEKADMIIYVVDNGQSVHFQTIFAAAQMIGWYDPK VTRVFHAGFGVVLGEDKKKFKTRSGETVRLMDLLGEGLKRSMDKLKEKERDKVLTAEELN AAQTSVAYGCIKYADLSHNRLNDYIFSFDKMLDDRGNTAAYLLYAFTRIRSIARLANIDE EMLQKAARETKILLDHEKEWKLGRCILRFPEILQKILDDLFLHTLCDYIYELATAFTEFY DSCYCVEKDRQTGKILKVNMWRMLLCEAVAAVMAKGFDILGIKPVQRMENLYFQSHHHHH H
2.2 Angstrom crystal structure of a human Arginyl-tRNA synthetase. Smith, A.T., Rosenzweig, A.C. To be published.
Other PDB entries of the same protein (UniProt P54136 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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