8RXB: Human UPF1 CH domain
Human UPF1 CH domain in complex with SMG6 peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 May 2024.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 7,195
- Mol. weight
- 127.39 kDa
- Ligands
- ZN
- Released
- 15 May 2024
Explore 8RXB in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8RXB contains 32 α-helices and 62 β-strands across 12 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: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 4 |
| β-strand | 28-31 | 4 | 4 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 4 |
| β-strand | 65-66 | 2 | 4 |
| β-strand | 80-84 | 5 | 5 |
| β-strand | 90-95 | 6 | 5 |
| β-strand | 116-117 | 2 | 5 |
| β-strand | 119-120 | 2 | 6 |
| β-strand | 123-124 | 2 | 6 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-138 | 5 | |
| α-helix | 141-142 | 2 | |
| α-helix | 145-157 | 13 | |
Chains B, F, G and N: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 408-410 | 3 | 5 |
Chain D: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 7 |
| β-strand | 28-31 | 4 | 7 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 7 |
| β-strand | 65-66 | 2 | 7 |
| β-strand | 80-83 | 4 | 8 |
| β-strand | 90-95 | 6 | 8 |
| β-strand | 116-117 | 2 | 8 |
| β-strand | 119-120 | 2 | 9 |
| β-strand | 123-124 | 2 | 9 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-139 | 6 | |
| α-helix | 141-142 | 2 | |
| α-helix | 145-155 | 11 | |
Chain E: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 1 |
| β-strand | 28-31 | 4 | 1 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 1 |
| β-strand | 65-66 | 2 | 1 |
| β-strand | 80-84 | 5 | 2 |
| β-strand | 90-95 | 6 | 2 |
| β-strand | 116-117 | 2 | 2 |
| β-strand | 119-120 | 2 | 3 |
| β-strand | 123-124 | 2 | 3 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-139 | 6 | |
| α-helix | 141-142 | 2 | |
| α-helix | 145-154 | 10 | |
Chain I: 6 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-19 | 3 | |
| β-strand | 20-23 | 4 | 10 |
| β-strand | 28-31 | 4 | 10 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 10 |
| β-strand | 65-66 | 2 | 10 |
| β-strand | 80-82 | 3 | 11 |
| β-strand | 91-92 | 2 | 12 |
| β-strand | 93-95 | 3 | 11 |
| β-strand | 116-117 | 2 | 11 |
| β-strand | 119-120 | 2 | 13 |
| β-strand | 123-124 | 2 | 13 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-138 | 5 | |
| α-helix | 141-142 | 2 | |
| α-helix | 145-154 | 10 | |
Chain J: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 408-409 | 2 | 12 |
Chain L: 5 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-19 | 3 | |
| β-strand | 20-23 | 4 | 14 |
| β-strand | 28-31 | 4 | 14 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 14 |
| β-strand | 65-66 | 2 | 14 |
| β-strand | 80-82 | 3 | 15 |
| β-strand | 90-92 | 3 | 16 |
| β-strand | 93-95 | 3 | 15 |
| β-strand | 116-117 | 2 | 15 |
| β-strand | 119-120 | 2 | 17 |
| β-strand | 123-124 | 2 | 17 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-138 | 5 | |
| α-helix | 145-154 | 10 | |
Chain P: 5 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 20-23 | 4 | 18 |
| β-strand | 28-31 | 4 | 18 |
| α-helix | 41-49 | 9 | |
| β-strand | 54-56 | 3 | 18 |
| β-strand | 66 | 1 | 18 |
| β-strand | 80-84 | 5 | 19 |
| β-strand | 91-95 | 5 | 19 |
| β-strand | 116-117 | 2 | 19 |
| β-strand | 119-120 | 2 | 20 |
| β-strand | 123-124 | 2 | 20 |
| α-helix | 130-133 | 4 | |
| α-helix | 134-139 | 6 | |
| α-helix | 141-142 | 2 | |
| α-helix | 145-155 | 11 | |
1 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Regulator of nonsense transcripts 1 | A, D, E, I, L, P | protein | 173 | Homo sapiens | Q92900 (AlphaFold model) |
| Telomerase-binding protein EST1A | B, F, G, J, N, Q | protein | 15 | Homo sapiens | Q86US8 (AlphaFold model) |
Sequence of entity 1 (A, D, E, I, L, P), FASTA
>8RXB_1 Regulator of nonsense transcripts 1 (chains A, D, E, I, L, P)
TKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDG
PLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQ
DRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDE
Sequence of entity 2 (B, F, G, J, N, Q), FASTA
>8RXB_2 Telomerase-binding protein EST1A (chains B, F, G, J, N, Q)
RGRGILILPAHTTLS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 13 |
Primary citation
UPF1 helicase orchestrates mutually exclusive interactions with the SMG6 endonuclease and UPF2. Langer, L.M., Kurscheidt, K., Basquin, J. et al. Nucleic Acids Res (2024) 52:6036-6048. DOI 10.1093/nar/gkae323 · PubMed
Other PDB entries of the same protein (UniProt Q92900 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2XZO 2.4 Å, Upf1 helicase - RNA complex
- 2GK6 2.4 Å, Structural and Functional insights into the human Upf1 helicase core
- 2WJY 2.5 Å, Crystal structure of the complex between human nonsense mediated decay factors UPF1 and…
- 2GJK 2.6 Å, Structural and functional insights into the human Upf1 helicase core
- 2XZP 2.72 Å, Upf1 helicase
- 2GK7 2.8 Å, Structural and Functional insights into the human Upf1 helicase core
- 2WJV 2.85 Å, Crystal structure of the complex between human nonsense mediated decay factors UPF1 and…
- 2IYK 2.95 Å, Crystal structure of the UPF2-interacting domain of nonsense mediated mRNA decay factor…
- 6Z3R 2.97 Å, Structure of SMG1-8-9 kinase complex bound to UPF1-LSQ
- 6EJ5 3.34 Å, A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity…
- 9QWN 3.6 Å, Human UPF1 in complex with the histone stem loop RNA
Browse structure collections
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