Crystal structure of human prolyl-tRNA synthetase (substrate bound form). Determined by X-ray diffraction at 2.3 Å resolution. Released 9 Oct 2013.
Explore 4K87 in 3D Show helices and sheets RCSB PDB PDBe
4K87 contains 21 α-helices and 31 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 | 24-34 | 11 | |
| β-strand | 38-40 | 3 | 1 |
| β-strand | 47-49 | 3 | 1 |
| α-helix | 51-70 | 20 | |
| β-strand | 74-75 | 2 | 2 |
| β-strand | 81-83 | 3 | 3 |
| α-helix | 84-88 | 5 | |
| α-helix | 91-97 | 7 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 3 |
| β-strand | 110-118 | 9 | 3 |
| α-helix | 119 | 1 | |
| α-helix | 123-133 | 11 | |
| α-helix | 137-139 | 3 | |
| β-strand | 142-151 | 10 | 2 |
| α-helix | 157-158 | 2 | |
| β-strand | 159 | 1 | 4 |
| β-strand | 163 | 1 | 4 |
| β-strand | 166-176 | 11 | 2 |
| α-helix | 180-195 | 16 | |
| α-helix | 196-200 | 5 | |
| β-strand | 206-209 | 4 | 2 |
| β-strand | 221-228 | 8 | 2 |
| β-strand | 235-245 | 11 | 2 |
| α-helix | 247-252 | 6 | |
| β-strand | 255-257 | 3 | 5 |
| β-strand | 265-267 | 3 | 5 |
| β-strand | 269-276 | 8 | 2 |
| α-helix | 278-287 | 10 | |
| β-strand | 289 | 1 | 6 |
| β-strand | 292 | 1 | 6 |
| β-strand | 304-308 | 5 | 7 |
| α-helix | 319-336 | 18 | |
| β-strand | 341-343 | 3 | 7 |
| α-helix | 351-361 | 11 | |
| β-strand | 365-369 | 5 | 7 |
| α-helix | 371-375 | 5 | |
| β-strand | 378-383 | 6 | 7 |
| β-strand | 389-393 | 5 | 7 |
| α-helix | 394-396 | 3 | |
| α-helix | 397-421 | 25 | |
| β-strand | 424-426 | 3 | 8 |
| α-helix | 430-436 | 7 | |
| β-strand | 442-447 | 6 | 8 |
| α-helix | 451-464 | 14 | |
| β-strand | 477-480 | 4 | 8 |
| β-strand | 481-482 | 2 | 2 |
| β-strand | 494 | 1 | 9 |
| β-strand | 501 | 1 | 9 |
| α-helix | 502 | 1 | |
| β-strand | 504-509 | 6 | 8 |
| β-strand | 511 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proline--tRNA ligase | A | protein | 535 | Homo sapiens | P07814 (AlphaFold model) |
>4K87_1 Proline--tRNA ligase (chains A) MGSSHHHHHHSSGLVPRGSHMASGAGEGQGPKKQTRLGLEAKKEENLADWYSQVITKSEM IEYHDISGCYILRPWAYAIWEAIKDFFDAEIKKLGVENCYFPMFVSQSALEKEKTHVADF APEVAWVTRSGKTELAEPIAIRPTSETVMYPAYAKWVQSHRDLPIKLNQWCNVVRWEFKH PQPFLRTREFLWQEGHSAFATMEEAAEEVLQILDLYAQVYEELLAIPVVKGRKTEKEKFA GGDYTTTIEAFISASGRAIQGGTSHHLGQNFSKMFEIVFEDPKIPGEKQFAYQNSWGLTT RTIGVMTMVHGDNMGLVLPPRVACVQVVIIPCGITNALSEEDKEALIAKCNDYRRRLLSV NIRVRADLRDNYSPGWKFNHWELKGVPIRLEVGPRDMKSCQFVAVRRDTGEKLTVAENEA ETKLQAILEDIQVTLFTRASEDLKTHMVVANTMEDFQKILDSGKIVQIPFCGEIDCEDWI KKTTARDQDLEPGAPSMGAKSLCIPFKPLCELQPGAKCVCGKNPAKYYTLFGRSY
Conformational changes in human prolyl-tRNA synthetase upon binding of the substrates proline and ATP and the inhibitor halofuginone. Son, J., Lee, E.H., Park, M. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:2136-2145. DOI 10.1107/S0907444913020556 · PubMed
Other PDB entries of the same protein (UniProt P07814 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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