Research workbench
MS2 (N87AE89K mutant) - qbeta RNA hairpin complex
Analyse MS2 (N87AE89K mutant) - qbeta RNA hairpin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BS1
- Type
- protein + RNA
- Length
- 410 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MS2 coat protein; 5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP *UP*AP*CP*CP*CP*AP*UP*GP*U)-3'
- UniProt
- P03612
- Pockets
- 5 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | MS2 coat protein | protein | 129 | 19% helix, 47% strand | P03612 |
| R | 5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP *UP*AP*CP*CP*CP*AP*UP*GP*U)-3' | rna | 12 | — | — |
| S | 5'-R(*AP*CP*AP*UP*GP*AP*GP*GP*AP*UP *UP*AP*CP*CP*CP*AP*UP*GP*U)-3' | rna | 11 | — | — |
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 | 474 | 0.67 | 0.79 | 55 | empty |
| 2 | 502 | 0.63 | 0.75 | 55 | empty |
| 3 | 224 | 0.54 | 0.78 | 30 | empty |
| 4 | 90 | 0.35 | 0.75 | 17 | empty |
| 5 | 56 | 0.26 | 0.74 | 14 | empty |
Interfaces
5 interfaces between chains.
- A–B · 3308 Ų buried · 44 hydrogen bonds · protein-protein
- A–C · 518 Ų buried · 9 hydrogen bonds · protein-protein
- A–R · 337 Ų buried · 7 hydrogen bonds · protein-nucleic
- C–S · 333 Ų buried · 8 hydrogen bonds · protein-nucleic
- B–R · 266 Ų buried · 12 hydrogen bonds · protein-nucleic
Compared structures
- 2BS1 · MS2 (N87AE89K mutant) - Qbeta RNA hairpin 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 2BS1 · PDBe 2BS1 · UniProt P03612
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