The 2.9 Å crystal structure of T. Thermophilus seryl-tRNA synthetase complexed with tRNA ser. Determined by X-ray diffraction at 2.9 Å resolution. Released 30 Apr 1994.
Explore 1SER in 3D Show helices and sheets RCSB PDB PDBe
1SER contains 50 α-helices and 40 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 | 4-9 | 6 | |
| α-helix | 11-21 | 11 | |
| α-helix | 27-36 | 10 | |
| α-helix | 90-98 | 9 | |
| α-helix | 101-106 | 6 | |
| α-helix | 110-111 | 2 | |
| α-helix | 114-116 | 3 | |
| β-strand | 118-123 | 6 | 1 |
| α-helix | 132-135 | 4 | |
| α-helix | 136-143 | 8 | |
| β-strand | 146 | 1 | 2 |
| α-helix | 150-154 | 5 | |
| β-strand | 161-162 | 2 | 2 |
| α-helix | 164-182 | 19 | |
| α-helix | 185 | 1 | |
| β-strand | 186-189 | 4 | 1 |
| β-strand | 193-195 | 3 | 3 |
| α-helix | 196-202 | 7 | |
| α-helix | 209-211 | 3 | |
| α-helix | 213 | 1 | |
| β-strand | 214 | 1 | 3 |
| β-strand | 215 | 1 | 4 |
| β-strand | 220-222 | 3 | 3 |
| α-helix | 227-233 | 7 | |
| β-strand | 238-240 | 3 | 5 |
| α-helix | 241-243 | 3 | |
| α-helix | 244 | 1 | |
| β-strand | 246-255 | 10 | 1 |
| β-strand | 274-284 | 11 | 1 |
| α-helix | 288-309 | 22 | |
| β-strand | 313-317 | 5 | 1 |
| α-helix | 318-319 | 2 | |
| β-strand | 329-337 | 9 | 1 |
| α-helix | 338-340 | 3 | |
| β-strand | 342-351 | 10 | 1 |
| α-helix | 357-360 | 4 | |
| β-strand | 363-365 | 3 | 5 |
| β-strand | 371-373 | 3 | 5 |
| β-strand | 375-384 | 10 | 1 |
| α-helix | 386-394 | 9 | |
| β-strand | 396 | 1 | 6 |
| β-strand | 402-403 | 2 | 6 |
| α-helix | 406-408 | 3 | |
| α-helix | 409-412 | 4 | |
| β-strand | 416-417 | 2 | 6 |
| α-helix | 418-419 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 504-509 | 6 | |
| α-helix | 511-520 | 10 | |
| α-helix | 527-557 | 31 | |
| α-helix | 565-598 | 34 | |
| α-helix | 601-606 | 6 | |
| α-helix | 610-611 | 2 | |
| α-helix | 614-616 | 3 | |
| β-strand | 618-623 | 6 | 2 |
| α-helix | 632-635 | 4 | |
| α-helix | 636-642 | 7 | |
| β-strand | 646 | 1 | 1 |
| α-helix | 650-654 | 5 | |
| β-strand | 661-662 | 2 | 1 |
| α-helix | 664-682 | 19 | |
| β-strand | 686-689 | 4 | 2 |
| β-strand | 693-695 | 3 | 7 |
| α-helix | 696-702 | 7 | |
| α-helix | 709-711 | 3 | |
| β-strand | 714 | 1 | 7 |
| β-strand | 715 | 1 | 4 |
| β-strand | 720-722 | 3 | 7 |
| α-helix | 727-732 | 6 | |
| β-strand | 738-740 | 3 | 8 |
| α-helix | 741-743 | 3 | |
| β-strand | 746-755 | 10 | 2 |
| β-strand | 774-784 | 11 | 2 |
| α-helix | 788-808 | 21 | |
| β-strand | 813-817 | 5 | 2 |
| α-helix | 818-819 | 2 | |
| α-helix | 820-823 | 4 | |
| β-strand | 829-837 | 9 | 2 |
| α-helix | 838-840 | 3 | |
| β-strand | 842-851 | 10 | 2 |
| α-helix | 857-860 | 4 | |
| β-strand | 863-865 | 3 | 8 |
| β-strand | 871-873 | 3 | 8 |
| β-strand | 875-884 | 10 | 2 |
| α-helix | 886-894 | 9 | |
| β-strand | 896 | 1 | 9 |
| β-strand | 902-903 | 2 | 9 |
| α-helix | 906-908 | 3 | |
| α-helix | 909-912 | 4 | |
| β-strand | 916-917 | 2 | 9 |
| α-helix | 918-919 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trnaser | T | RNA | 94 | Thermus thermophilus | |
| Protein (seryl-tRNA synthetase (E.C.6.1.1.11)) | A, B | protein | 421 | Thermus thermophilus | P34945 (AlphaFold model) |
>1SER_1 TRNASER (chains T) GGAGAGGUGCCCGAGUGGCUGAAGGGACACGACUGGAAAUCGUGUAGGGGGGCUUAAACC UCCCUCGCGGGUUCGAAUCCCGCCCUCUCCGCCA
>1SER_2 PROTEIN (SERYL-TRNA SYNTHETASE (E.C.6.1.1.11)) (chains A, B) MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPK APPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPVGGEEANREI KRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFM ARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILP YEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLE NAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRA NLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPC G
The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser). Biou, V., Yaremchuk, A., Tukalo, M. et al. Science (1994) 263:1404-1410. PubMed
Other PDB entries of the same protein (UniProt P34945 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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