9QRP: Thermus thermophilus seryl-tRNA synthetase

Thermus thermophilus seryl-tRNA synthetase bound to tRNA(ser)(GGA) and seryl-adenylate analogue. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 May 2025.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Thermus thermophilus HB8
Chains
3
Atoms
8,846
Mol. weight
128.04 kDa
Ligands
MN, SSA
Released
14 May 2025

Explore 9QRP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9QRP contains 51 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, 19 β-strands

ElementResiduesLengthSheet
α-helix4-96
α-helix11-2111
α-helix27-4923
α-helix79-9820
α-helix101-1066
α-helix1101
α-helix114-1163
β-strand118-12361
α-helix125-1273
α-helix132-1354
α-helix136-1438
β-strand14612
α-helix150-1545
β-strand161-16222
α-helix163-18220
β-strand186-18941
β-strand193-19533
α-helix196-2027
α-helix204-2074
α-helix209-2113
β-strand214-21523
β-strand220-22233
α-helix227-2326
β-strand238-24034
α-helix241-2433
α-helix2441
β-strand246-255101
β-strand274-284111
α-helix288-30821
β-strand313-31751
α-helix318-3192
α-helix320-3223
β-strand329-33791
α-helix338-3403
β-strand342-351101
α-helix357-3604
β-strand363-36534
β-strand371-37334
β-strand375-384101
α-helix386-3949
β-strand39615
β-strand402-40325
α-helix406-4083
α-helix409-4124
β-strand416-41725
α-helix418-4192
Chain B: 24 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix4-96
α-helix11-2111
α-helix27-5731
α-helix63-9836
α-helix101-1066
α-helix110-1112
α-helix114-1163
β-strand118-12362
α-helix136-1438
β-strand14611
α-helix150-1545
β-strand161-16221
α-helix163-18119
β-strand186-18942
β-strand193-19533
α-helix196-2027
α-helix209-2113
β-strand213-21533
β-strand220-22233
α-helix227-2326
β-strand237-24046
α-helix241-2433
α-helix2441
β-strand246-255102
β-strand274-284112
α-helix288-30821
β-strand313-31752
α-helix318-3192
α-helix320-3234
β-strand329-33792
α-helix338-3403
β-strand342-351102
α-helix355-3606
β-strand362-36546
β-strand371-37336
β-strand375-384102
α-helix386-3949
β-strand39617
β-strand40217
β-strand40318
α-helix406-4083
α-helix409-4124
β-strand41618
α-helix417-4193

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine--tRNA ligaseA, Bprotein421Thermus thermophilus HB8P34945 (AlphaFold model)
tRNA(Ser), GGA anticodonTRNA94Thermus thermophilus HB8
Sequence of entity 1 (A, B), FASTA
>9QRP_1 Serine--tRNA ligase (chains A, B)
MVDLKRLRQEPEVFHRAIREKGVALDLEALLALDREVQELKKRLQEVQTERNQVAKRVPK
APPEEKEALIARGKALGEEAKRLEEALREKEARLEALLLQVPLPPWPGAPVGGEEANREI
KRVGGPPEFSFPPLDHVALMEKNGWWEPRISQVSGSRSYALKGDLALYELALLRFAMDFM
ARRGFLPMTLPSYAREKAFLGTGHFPAYRDQVWAIAETDLYLTGTAEVVLNALHSGEILP
YEALPLRYAGYAPAFRSEAGSFGKDVRGLMRVHQFHKVEQYVLTEASLEASDRAFQELLE
NAEEILRLLELPYRLVEVATGDMGPGKWRQVDIEVYLPSEGRYRETHSCSALLDWQARRA
NLRYRDPEGRVRYAYTLNNTALATPRILAMLLENHQLQDGRVRVPQALIPYMGKEVLEPC
G
Sequence of entity 2 (T), FASTA
>9QRP_2 tRNA(Ser), GGA anticodon (chains T)
GGAGAGGUGCCCGAGUGGCUGAAGGGACACGACUGGAAAUCGUGUAGGGGGGCUUAAACC
UCCCUCGCGGGUUCGAAUCCCGCCCUCUCCGCCA

Ligands and cofactors

IDNameFormulaCopies
MNManganese (II) ionMn1
SSA5'-O-(N-(L-seryl)-sulfamoyl)adenosineC13 H19 N7 O8 S2

Water and common crystallization additives (SO4) are not listed.

Primary citation

The crystal structure of the ternary complex of T.thermophilus seryl-tRNA synthetase with tRNA(Ser) and a seryl-adenylate analogue reveals a conformational switch in the active site. Cusack, S., Yaremchuk, A., Tukalo, M. EMBO J (1996) 15:2834-2842. 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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