Crystal structures at 2.5 Å resolution of seryl-tRNA synthetase complexed with two different analogues of seryl-adenylate. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 Jul 1994.
Explore 1SES in 3D Show helices and sheets RCSB PDB PDBe
1SES contains 55 α-helices and 39 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 | 27-57 | 31 | |
| α-helix | 63-98 | 36 | |
| α-helix | 101-106 | 6 | |
| α-helix | 110 | 1 | |
| α-helix | 114-116 | 3 | |
| α-helix | 117 | 1 | |
| β-strand | 118-123 | 6 | 1 |
| α-helix | 125-127 | 3 | |
| 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 | 227-232 | 6 | |
| β-strand | 238-240 | 3 | 5 |
| α-helix | 241-243 | 3 | |
| β-strand | 246-255 | 10 | 1 |
| β-strand | 274-284 | 11 | 1 |
| α-helix | 288-308 | 21 | |
| β-strand | 313-317 | 5 | 1 |
| α-helix | 320-323 | 4 | |
| β-strand | 329-337 | 9 | 1 |
| β-strand | 342-353 | 12 | 1 |
| α-helix | 355-360 | 6 | |
| β-strand | 363-365 | 3 | 5 |
| β-strand | 371-373 | 3 | 5 |
| β-strand | 375-384 | 10 | 1 |
| α-helix | 386-395 | 10 | |
| β-strand | 396 | 1 | 6 |
| β-strand | 402-403 | 2 | 6 |
| α-helix | 404-405 | 2 | |
| 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 | 4-9 | 6 | |
| α-helix | 11-21 | 11 | |
| α-helix | 27-57 | 31 | |
| α-helix | 58-60 | 3 | |
| α-helix | 63-98 | 36 | |
| α-helix | 101-106 | 6 | |
| α-helix | 110-111 | 2 | |
| α-helix | 114-116 | 3 | |
| β-strand | 118-123 | 6 | 2 |
| α-helix | 132-135 | 4 | |
| α-helix | 136-143 | 8 | |
| β-strand | 146 | 1 | 1 |
| α-helix | 150-153 | 4 | |
| β-strand | 161-162 | 2 | 1 |
| α-helix | 164-182 | 19 | |
| α-helix | 185 | 1 | |
| β-strand | 186-189 | 4 | 2 |
| β-strand | 193-195 | 3 | 4 |
| α-helix | 196-202 | 7 | |
| α-helix | 209-211 | 3 | |
| α-helix | 213 | 1 | |
| β-strand | 214-215 | 2 | 4 |
| β-strand | 220-222 | 3 | 4 |
| α-helix | 226-232 | 7 | |
| β-strand | 238-240 | 3 | 7 |
| α-helix | 241-243 | 3 | |
| α-helix | 244 | 1 | |
| β-strand | 246-255 | 10 | 2 |
| β-strand | 274-284 | 11 | 2 |
| α-helix | 288-309 | 22 | |
| β-strand | 313-317 | 5 | 2 |
| α-helix | 318-319 | 2 | |
| α-helix | 320-323 | 4 | |
| β-strand | 329-337 | 9 | 2 |
| α-helix | 338-340 | 3 | |
| β-strand | 342-351 | 10 | 2 |
| α-helix | 357-360 | 4 | |
| β-strand | 363-365 | 3 | 7 |
| β-strand | 371-373 | 3 | 7 |
| β-strand | 375-384 | 10 | 2 |
| α-helix | 386-395 | 10 | |
| β-strand | 396 | 1 | 8 |
| β-strand | 402-403 | 2 | 8 |
| α-helix | 406-408 | 3 | |
| α-helix | 409-412 | 4 | |
| β-strand | 416-417 | 2 | 8 |
| α-helix | 418-419 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Seryl-tRNA synthetase | A, B | protein | 421 | Thermus thermophilus | P34945 (AlphaFold model) |
>1SES_1 SERYL-tRNA SYNTHETASE (chains A, B) MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPK APPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPVGGEEANREI KRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFM ARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILP YEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLE NAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRA NLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPC G
| ID | Name | Formula | Copies |
|---|---|---|---|
| AHX | Seryl-hydroxamate-adenosine monophosphate | C13 H20 N7 O9 P | 1 |
| AMP | Adenosine monophosphate | C10 H14 N5 O7 P | 1 |
Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate. Belrhali, H., Yaremchuk, A., Tukalo, M. et al. Science (1994) 263:1432-1436. 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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