1SES: Crystal structures

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.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Thermus thermophilus
Chains
2
Atoms
6,929
Mol. weight
96.55 kDa
Ligands
AHX, AMP
Released
31 Jul 1994

Explore 1SES in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 27 helices, 20 β-strands

ElementResiduesLengthSheet
α-helix4-96
α-helix11-2111
α-helix27-5731
α-helix63-9836
α-helix101-1066
α-helix1101
α-helix114-1163
α-helix1171
β-strand118-12361
α-helix125-1273
α-helix132-1354
α-helix136-1438
β-strand14612
α-helix150-1545
β-strand161-16222
α-helix164-18219
α-helix1851
β-strand186-18941
β-strand193-19533
α-helix196-2027
α-helix209-2113
α-helix2131
β-strand21413
β-strand21514
β-strand220-22233
α-helix227-2326
β-strand238-24035
α-helix241-2433
β-strand246-255101
β-strand274-284111
α-helix288-30821
β-strand313-31751
α-helix320-3234
β-strand329-33791
β-strand342-353121
α-helix355-3606
β-strand363-36535
β-strand371-37335
β-strand375-384101
α-helix386-39510
β-strand39616
β-strand402-40326
α-helix404-4052
α-helix406-4083
α-helix409-4124
β-strand416-41726
α-helix418-4192
Chain B: 28 helices, 19 β-strands
ElementResiduesLengthSheet
α-helix4-96
α-helix11-2111
α-helix27-5731
α-helix58-603
α-helix63-9836
α-helix101-1066
α-helix110-1112
α-helix114-1163
β-strand118-12362
α-helix132-1354
α-helix136-1438
β-strand14611
α-helix150-1534
β-strand161-16221
α-helix164-18219
α-helix1851
β-strand186-18942
β-strand193-19534
α-helix196-2027
α-helix209-2113
α-helix2131
β-strand214-21524
β-strand220-22234
α-helix226-2327
β-strand238-24037
α-helix241-2433
α-helix2441
β-strand246-255102
β-strand274-284112
α-helix288-30922
β-strand313-31752
α-helix318-3192
α-helix320-3234
β-strand329-33792
α-helix338-3403
β-strand342-351102
α-helix357-3604
β-strand363-36537
β-strand371-37337
β-strand375-384102
α-helix386-39510
β-strand39618
β-strand402-40328
α-helix406-4083
α-helix409-4124
β-strand416-41728
α-helix418-4192

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Seryl-tRNA synthetaseA, Bprotein421Thermus thermophilusP34945 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1SES_1 SERYL-tRNA SYNTHETASE (chains A, B)
MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPK
APPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPVGGEEANREI
KRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFM
ARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILP
YEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLE
NAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRA
NLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPC
G

Ligands and cofactors

IDNameFormulaCopies
AHXSeryl-hydroxamate-adenosine monophosphateC13 H20 N7 O9 P1
AMPAdenosine monophosphateC10 H14 N5 O7 P1

Primary citation

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:

Browse structure collections

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