Research workbench
MS2-RNA hairpin (C-7) complex
Analyse MS2-RNA hairpin (C-7) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IZ8
- Type
- protein + RNA
- Length
- 416 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MS2 coat protein; RNA, (5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*CP*UP*CP*…
- UniProt
- P03612
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | MS2 coat protein | protein | 129 | 18% helix, 47% strand | P03612 |
| R | RNA, (5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*CP*UP*CP* AP*CP*CP*CP*AP*UP*GP*U)-3') | rna | 16 | — | — |
| S | RNA, (5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*CP*UP*CP* AP*CP*CP*CP*AP*UP*GP*U)-3') | rna | 13 | — | — |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.67 | 0.80 | 39 | empty |
| 2 | 486 | 0.62 | 0.75 | 53 | empty |
| 3 | 387 | 0.61 | 0.77 | 45 | empty |
| 4 | 112 | 0.37 | 0.74 | 24 | empty |
| 5 | 96 | 0.30 | 0.72 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3323 Ų buried · 42 hydrogen bonds · protein-protein
- A–C · 510 Ų buried · 4 hydrogen bonds · protein-protein
- B–R · 433 Ų buried · 16 hydrogen bonds · protein-nucleic
- C–S · 357 Ų buried · 11 hydrogen bonds · protein-nucleic
- A–R · 353 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 2IZ8 · MS2-RNA hairpin (C-7) complex · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P03612
- Elsewhere: RCSB PDB 2IZ8 · PDBe 2IZ8 · UniProt P03612
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