1DT9: Protein

The crystal structure of human eukaryotic release factor ERF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Determined by X-ray diffraction at 2.7 Å resolution. Released 2 Feb 2000.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,241
Mol. weight: 49.09 kDa
Released: 2 Feb 2000

Explore 1DT9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DT9 contains 14 α-helices and 16 β-strands across 1 chain. 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: 14 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	10-25	16
β-strand	34-39	6	1
α-helix	45-59	15
α-helix	66-82	17
β-strand	93-101	9	1
α-helix	103-105	3
β-strand	107-114	8	1
β-strand	124-128	5	1
α-helix	134-139	6
α-helix	143-144	2
β-strand	145-150	6	2
β-strand	158-162	5	2
β-strand	165-170	6	2
α-helix	188-197	10
α-helix	204-208	5
β-strand	225-228	4	2
α-helix	234-237	4
β-strand	253-255	3	2
α-helix	262-271	10
α-helix	278-295	18
β-strand	301-303	3	3
α-helix	305-313	9
β-strand	319-323	5	3
β-strand	329	1	4
β-strand	346	1	4
β-strand	373	1	4
α-helix	374-380	7
β-strand	389-392	4	3
α-helix	397-404	8
β-strand	409-412	4	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (eukaryotic peptide chain release factor subunit 1)	A	protein	437	Homo sapiens	P62495 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1DT9_1 PROTEIN (EUKARYOTIC PEPTIDE CHAIN RELEASE FACTOR SUBUNIT 1) (chains A)
MADDPSAADRNVEIWKIKKLIKSLEAARGNGTSMISLIIPPKDQISRVAKMLADEFGTAS
NIKSRVNRLSVLGAITSVQQRLKLYNKVPPNGLVVYCGTIVTEEGKEKKVNIDFEPFKPI
NTSLYLCDNKFHTEALTALLSDDSKFGFIVIDGSGALFGTLQGNTREVLHKFTVDLPKKH
GRGGQSALRFARLRMEKRHNYVRKVAETAVQLFISGDKVNVAGLVLAGSADFKTELSQSD
MFDQRLQSKVLKLVDISYGGENGFNQAIELSTEVLSNVKFIQEKKLIGRYFDEISQDTGK
YCFGVEDTLKALEMGAVEILIVYENLDIMRYVLHCQGTEEEKILYLTPEQEKDKSHFTDK
ETGQEHELIESMPLLEWFANNYKKFGATLEIVTDKSQEGSQFVKGFGGIGGILRYRVDFQ
GMEYQGGDDEFFDLDDY

Primary citation

The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Song, H., Mugnier, P., Das, A.K. et al. Cell (2000) 100:311-321. DOI 10.1016/S0092-8674(00)80667-4 · PubMed

Other PDB entries of the same protein (UniProt P62495 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9I2D 2.19 Å, NMT1-NAC bound human RNC with 10 amino acid ARF1-linker
8ZHC 2.3 Å, pre-frameshift complex of yeast 80S ribosome with eRF1 and mRNA of WNV
9S3D 2.32 Å, NAC bound human RNC with 58 amino acid ARF1-linker
9S3B 2.38 Å, NMT1-NAC bound human RNC with 58 amino acid ARF1-linker - State 1
9S3C 2.42 Å, NMT1-NAC bound human RNC with 58 amino acid ARF1-linker - State 2
9QLO 2.47 Å, NMT1-NAC bound human RNC with full length ARF1 - State 1
8SCB 2.5 Å, Terminating ribosome with SRI-41315
9QLQ 2.57 Å, NMT1-NAC bound human RNC with full length ARF1 - alternative State
9RHU 2.65 Å, Rabbit 80S ribosome in complex with eRF1-AAQ, stalled at the Stop codon in mutated F2A…
9QLP 2.75 Å, NMT1-NAC bound human RNC with full length ARF1 - State 2
6XA1 2.8 Å, Structure of a drug-like compound stalled human translation termination complex
6ZME 3.0 Å, SARS-CoV-2 Nsp1 bound to the human CCDC124-80S-eERF1 ribosome complex

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