1ASY: Aspartyl-tRNA synthetase

Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA asp. Determined by X-ray diffraction at 2.9 Å resolution. Released 8 May 1995.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 11,096
Mol. weight: 160.42 kDa
Released: 8 May 1995

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

Secondary structure: helices and β-sheets

1ASY contains 47 α-helices and 51 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: 25 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	75-77	3	1
α-helix	78-79	2
α-helix	91-95	5
α-helix	96-98	3
β-strand	110-122	13	1
β-strand	125-131	7	1
β-strand	136-142	7	1
α-helix	151-158	8
α-helix	160-161	2
β-strand	165-174	10	1
α-helix	175	1
β-strand	187-198	12	1
α-helix	208-212	5
α-helix	215-219	5
α-helix	228-233	6
α-helix	235-238	4
α-helix	244-264	21
β-strand	268-269	2	2
β-strand	275-276	2	3
α-helix	287	1
β-strand	288	1	3
β-strand	289-290	2	4
β-strand	291	1	5
β-strand	294	1	5
β-strand	297-298	2	3
α-helix	303-311	9
β-strand	316-323	8	2
β-strand	338-346	9	2
α-helix	352-372	21
α-helix	374-381	8
β-strand	398-401	4	2
α-helix	402-411	10
α-helix	421-423	3
α-helix	424-438	15
β-strand	442-446	5	2
α-helix	448	1
β-strand	449	1	6
β-strand	457	1	2
α-helix	458	1
β-strand	459	1	7
α-helix	460	1
β-strand	466	1	6
β-strand	467	1	7
β-strand	470-474	5	2
β-strand	477-485	9	2
α-helix	489-498	10
α-helix	506-513	8
β-strand	522-528	7	2
α-helix	529-537	9
α-helix	542-545	4

Chain B: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	75-77	3	8
α-helix	96-98	3
α-helix	101-104	4
β-strand	108-119	12	8
β-strand	127-131	5	8
β-strand	136-140	5	8
α-helix	151-158	8
β-strand	165-174	10	8
β-strand	187-198	12	8
α-helix	208-212	5
α-helix	215-220	6
α-helix	228-233	6
α-helix	235-239	5
α-helix	242-254	13
α-helix	258-262	5
α-helix	263-265	3
β-strand	275-276	2	4
β-strand	288-291	4	4
β-strand	294-298	5	4
α-helix	303-311	9
β-strand	319-324	6	9
β-strand	331	1	10
β-strand	334	1	10
β-strand	337-342	6	9
α-helix	352-381	30
α-helix	387-389	3
β-strand	398-400	3	11
α-helix	402-410	9
α-helix	421-423	3
α-helix	424-438	15
β-strand	442-445	4	11
β-strand	449	1	12
β-strand	457	1	13
α-helix	458	1
β-strand	459-460	2	14
β-strand	463-467	5	14
β-strand	469-474	6	11
β-strand	477-483	7	11
β-strand	484	1	15
β-strand	485	1	13
α-helix	489-498	10
α-helix	506-516	11
β-strand	523	1	15
β-strand	526	1	11
β-strand	528	1	9
α-helix	529-533	5
α-helix	534-538	5
α-helix	542-545	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
T-RNA (75-mer)	R, S	RNA	75
Aspartyl-tRNA synthetase	A, B	protein	490	Saccharomyces cerevisiae	P04802 (AlphaFold model)

Sequence of entity 1 (R, S), FASTA

>1ASY_1 T-RNA (75-MER) (chains R, S)
UCCGUGAUAGUUUAAUGGUCAGAAUGGGCGCUUGUCGCGUGCCAGAUCGGGGUUCAAUUC
CCCGUCGCGGAGCCA

Sequence of entity 2 (A, B), FASTA

>1ASY_2 ASPARTYL-tRNA SYNTHETASE (chains A, B)
EDTAKDNYGKLPLIQSRDSDRTGQKRVKFVDLDEAKDSDKEVLFRARVHNTRQQGATLAF
LTLRQQASLIQGLVKANKEGTISKNMVKWAGSLNLESIVLVRGIVKKVDEPIKSATVQNL
EIHITKIYTISETPEALPILLEDASRSEAEAEAAGLPVVNLDTRLDYRVIDLRTVTNQAI
FRIQAGVCELFREYLATKKFTEVHTPKLLGAPSEGGSSVFEVTYFKGKAYLAQSPQFNKQ
QLIVADFERVYEIGPVFRAENSNTHRHMTEFTGLDMEMAFEEHYHEVLDTLSELFVFIFS
ELPKRFAHEIELVRKQYPVEEFKLPKDGKMVRLTYKEGIEMLRAAGKEIGDFEDLSTENE
KFLGKLVRDKYDTDFYILDKFPLEIRPFYTMPDPANPKYSNSYDFFMRGEEILSGAQRIH
DHALLQERMKAHGLSPEDPGLKDYCDGFSYGCPPHAGGGIGLERVVMFYLDLKNIRRASL
FPRDPKRLRP

Primary citation

Class II aminoacyl transfer RNA synthetases: crystal structure of yeast aspartyl-tRNA synthetase complexed with tRNA(Asp). Ruff, M., Krishnaswamy, S., Boeglin, M. et al. Science (1991) 252:1682-1689. PubMed

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

1EOV 2.3 Å, Free aspartyl-tRNA synthetase (ASPRS) (e.c. 6.1.1.12) from yeast
1ASZ 3.0 Å, The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of…

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1ASY is part of these collections:

The ribosome and protein synthesis

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