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Crystal structure of B.SUBTILIS anti-trap protein, an antagonist of trap-RNA interactions
Analyse Crystal structure of B.SUBTILIS anti-trap protein, an antagonist of trap-RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BX9
- Type
- protein
- Length
- 636 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan RNA-binding attenuator protein-inhibitory protein
- UniProt
- O31466
- Ligands
- ZN
- Pockets
- 12 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Tryptophan RNA-binding attenuator protein-inhibitory protein | protein | 53 | 32% helix, 19% strand | O31466 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 350 | 0.80 | 0.90 | 34 | empty |
| 2 | 50 | 0.66 | 0.96 | 17 | empty |
| 3 | 52 | 0.64 | 0.94 | 18 | empty |
| 4 | 84 | 0.41 | 0.78 | 23 | empty |
| 5 | 93 | 0.37 | 0.75 | 24 | empty |
Interfaces
34 interfaces between chains.
- A–B · 699 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 698 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 692 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 691 Ų buried · 6 hydrogen bonds · protein-protein
- D–F · 676 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2BX9 · Crystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactions · the same entry in another collection · chain L against L, 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 O31466
- Elsewhere: RCSB PDB 2BX9 · PDBe 2BX9 · UniProt O31466
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