2QFD: Regulatory domain of human RIG-I with bound Hg
Crystal structure of the regulatory domain of human RIG-I with bound Hg. Determined by X-ray diffraction at 2.7 Å resolution. Released 12 Feb 2008.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 10,092
- Mol. weight
- 170.54 kDa
- Ligands
- HG
- Released
- 12 Feb 2008
Explore 2QFD in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2QFD contains 56 α-helices and 111 β-strands across 10 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: 7 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 1 |
| β-strand | 816-819 | 4 | 1 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 2 |
| β-strand | 830-833 | 4 | 2 |
| α-helix | 838-840 | 3 | |
| β-strand | 842-846 | 5 | 3 |
| β-strand | 856-864 | 9 | 3 |
| β-strand | 872-879 | 8 | 3 |
| β-strand | 882-887 | 6 | 3 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 1 |
| β-strand | 902-904 | 3 | 1 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 2 |
| α-helix | 918 | 1 | |
| α-helix | 920-922 | 3 | |
Chain B: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 4 |
| β-strand | 816-819 | 4 | 4 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 5 |
| β-strand | 830-833 | 4 | 5 |
| α-helix | 838-840 | 3 | |
| β-strand | 842-846 | 5 | 6 |
| β-strand | 857-864 | 8 | 6 |
| β-strand | 872-879 | 8 | 6 |
| β-strand | 882-887 | 6 | 6 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 4 |
| β-strand | 902-904 | 3 | 4 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 5 |
| α-helix | 918 | 1 | |
Chain C: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 806-810 | 5 | 7 |
| β-strand | 816-819 | 4 | 7 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 8 |
| β-strand | 830-833 | 4 | 8 |
| α-helix | 836-839 | 4 | |
| β-strand | 842-845 | 4 | 9 |
| β-strand | 857-864 | 8 | 9 |
| β-strand | 872-879 | 8 | 9 |
| β-strand | 882-887 | 6 | 9 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-896 | 5 | 7 |
| β-strand | 902-903 | 2 | 7 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 8 |
| α-helix | 918 | 1 | |
Chain D: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 4 |
| β-strand | 816-819 | 4 | 4 |
| β-strand | 823-826 | 4 | 10 |
| β-strand | 830-833 | 4 | 10 |
| α-helix | 836-839 | 4 | |
| β-strand | 842-846 | 5 | 11 |
| β-strand | 857-864 | 8 | 11 |
| β-strand | 872-879 | 8 | 11 |
| β-strand | 882-887 | 6 | 11 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 4 |
| β-strand | 902-904 | 3 | 4 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 10 |
| α-helix | 918 | 1 | |
Chain E: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 806-810 | 5 | 1 |
| β-strand | 816-819 | 4 | 1 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 12 |
| β-strand | 830-833 | 4 | 12 |
| α-helix | 836-839 | 4 | |
| β-strand | 842-843 | 2 | 13 |
| β-strand | 857-864 | 8 | 13 |
| β-strand | 872-878 | 7 | 13 |
| β-strand | 883-887 | 5 | 13 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-896 | 5 | 1 |
| β-strand | 902-904 | 3 | 1 |
| α-helix | 908-910 | 3 | |
| β-strand | 917 | 1 | 12 |
Chain F: 7 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 14 |
| β-strand | 818-819 | 2 | 14 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 15 |
| β-strand | 830-833 | 4 | 15 |
| α-helix | 836-839 | 4 | |
| β-strand | 842-846 | 5 | 16 |
| α-helix | 847 | 1 | |
| β-strand | 852 | 1 | 16 |
| β-strand | 857-864 | 8 | 16 |
| β-strand | 872-879 | 8 | 16 |
| β-strand | 882-887 | 6 | 16 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 14 |
| β-strand | 902-903 | 2 | 14 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 15 |
| α-helix | 918 | 1 | |
Chain G: 5 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 17 |
| β-strand | 816-819 | 4 | 17 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 18 |
| β-strand | 830-833 | 4 | 18 |
| α-helix | 836-839 | 4 | |
| β-strand | 842-846 | 5 | 19 |
| β-strand | 857-864 | 8 | 19 |
| β-strand | 872-879 | 8 | 19 |
| β-strand | 882-887 | 6 | 19 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 17 |
| β-strand | 902-904 | 3 | 17 |
| α-helix | 908-910 | 3 | |
| β-strand | 916-917 | 2 | 18 |
| α-helix | 918 | 1 | |
Chain H: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 807-810 | 4 | 20 |
| β-strand | 816-819 | 4 | 20 |
| α-helix | 820-822 | 3 | |
| β-strand | 823-826 | 4 | 21 |
| β-strand | 830-833 | 4 | 21 |
| α-helix | 839-841 | 3 | |
| β-strand | 842-846 | 5 | 22 |
| β-strand | 857-864 | 8 | 22 |
| β-strand | 872-878 | 7 | 22 |
| β-strand | 883-887 | 5 | 22 |
| α-helix | 889-891 | 3 | |
| β-strand | 892-895 | 4 | 20 |
| β-strand | 902-903 | 2 | 20 |
| α-helix | 908-910 | 3 | |
| α-helix | 916 | 1 | |
| β-strand | 917 | 1 | 21 |
| α-helix | 918 | 1 | |
2 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 |
|---|
| Probable ATP-dependent RNA helicase DDX58 | A, B, C, D, E, F, G, H, I, J | protein | 145 | Homo sapiens | O95786 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J), FASTA
>2QFD_1 Probable ATP-dependent RNA helicase DDX58 (chains A, B, C, D, E, F, G, H, I, J)
MGSSHHHHHHSSGLVPRGSHMDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKE
CFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIESFVVEDIATG
VQTLYSKWKDFHFEKIPFDPAEMSK
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| HG | Mercury (II) ion | Hg | 10 |
Primary citation
The C-Terminal Regulatory Domain Is the RNA 5'-Triphosphate Sensor of RIG-I. Cui, S., Eisenacher, K., Kirchhofer, A. et al. Mol Cell (2008) 29:169-179. DOI 10.1016/j.molcel.2007.10.032 · PubMed
Other PDB entries of the same protein (UniProt O95786 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7BAH 1.89 Å, Structure of RIG-I CTD bound to OH-RNA
- 7MK1 1.9 Å, Structure of a protein-modified aptamer complex
- 3LRR 2.15 Å, Crystal structure of human RIG-I CTD bound to a 12 bp AU rich 5' ppp dsRNA
- 3OG8 2.4 Å, Crystal structure of human RIG-I CTD bound to a 14-bp blunt-ended dsRNA
- 9KU4 2.4 Å, Cryo-EM structure of E373A mutant RIG-I with 5'p-RNA
- 2YKG 2.5 Å, Structural insights into RNA recognition by RIG-I
- 3ZD7 2.5 Å, Snapshot 3 of RIG-I scanning on RNA duplex
- 3NCU 2.55 Å, Structural and functional insights into pattern recognition by the innate immune…
- 4BPB 2.58 Å, Structural insights into RNA recognition by rig-I
- 3LRN 2.6 Å, Crystal structure of human RIG-I CTD bound to a 14 bp GC 5' ppp dsRNA
- 9KTW 2.6 Å, Cryo-EM structure of wild type RIG-I with 5'p-RNA
- 5F9F 2.6 Å, Crystal structure of RIG-I helicase-RD in complex with 24-mer blunt-end hairpin RNA
Browse structure collections
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