1ASZ: Aspartyl-tRNA synthetase

The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. Determined by X-ray diffraction at 3.0 Å resolution. Released 8 May 1995.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Saccharomyces cerevisiae
Chains
4
Atoms
11,158
Mol. weight
161.43 kDa
Ligands
ATP
Released
8 May 1995

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

Secondary structure: helices and β-sheets

1ASZ contains 46 α-helices and 58 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: 24 helices, 26 β-strands

ElementResiduesLengthSheet
β-strand75-7731
α-helix93-953
α-helix96-983
β-strand108-122151
β-strand125-13281
β-strand135-14281
α-helix151-1599
α-helix160-1612
β-strand165-174101
β-strand187-196101
α-helix208-2125
α-helix215-2195
α-helix228-2325
α-helix235-2384
α-helix242-26423
β-strand268-26922
β-strand275-27623
β-strand28813
β-strand28914
β-strand29115
β-strand29415
β-strand297-29823
α-helix303-3119
β-strand316-32492
β-strand337-346102
α-helix352-36615
α-helix369-3724
α-helix374-3818
α-helix387-3904
β-strand398-40142
α-helix402-41110
α-helix420-4234
α-helix424-43815
β-strand442-44652
α-helix4481
β-strand44916
β-strand45717
α-helix4581
β-strand45918
α-helix4601
β-strand46616
β-strand46718
β-strand470-47452
β-strand477-48482
β-strand48517
α-helix489-49810
α-helix506-5138
β-strand522-52872
α-helix529-5379
α-helix543-5453
Chain B: 22 helices, 32 β-strands
ElementResiduesLengthSheet
α-helix70-734
β-strand75-7739
β-strand9419
α-helix96-983
α-helix101-1044
β-strand108-122159
β-strand125-13179
β-strand136-14059
α-helix151-1599
β-strand165-174109
β-strand187-198129
α-helix208-2125
α-helix215-2173
α-helix218-2225
α-helix228-2336
α-helix235-2395
α-helix242-26322
β-strand268-269210
β-strand27614
β-strand288-29144
β-strand293-29754
α-helix303-3119
β-strand317-324810
β-strand331111
β-strand334111
β-strand337-344810
α-helix352-37221
α-helix374-3818
α-helix396-3972
β-strand398-401412
α-helix402-4109
α-helix424-43714
β-strand442-446512
β-strand449113
β-strand457114
α-helix4581
β-strand459115
α-helix4601
β-strand466113
β-strand467115
β-strand469-474612
β-strand477-483712
β-strand484116
β-strand485114
α-helix489-49810
α-helix506-51611
β-strand523116
β-strand524-525210
β-strand526-527212
β-strand528110
α-helix529-5335
α-helix534-5385
β-strand551117
β-strand554117

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
T-RNA (75-mer)R, SRNA75
Aspartyl-tRNA synthetaseA, Bprotein490Saccharomyces cerevisiaeP04802 (AlphaFold model)
Sequence of entity 1 (R, S), FASTA
>1ASZ_1 T-RNA (75-MER) (chains R, S)
UCCGUGAUAGUUUAAUGGUCAGAAUGGGCGCUUGUCGCGUGCCAGAUCGGGGUUCAAUUC
CCCGUCGCGGAGCCA
Sequence of entity 2 (A, B), FASTA
>1ASZ_2 ASPARTYL-tRNA SYNTHETASE (chains A, B)
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAF
LTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAI
FRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFS
ELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIH
DHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32

Primary citation

The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction. Cavarelli, J., Eriani, G., Rees, B. et al. EMBO J (1994) 13:327-337. PubMed

Other PDB entries of the same protein (UniProt P04802 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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