Research workbench
The nature of the TRAP:ANTI-trap complex
Analyse The nature of the TRAP:ANTI-trap complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZP8
- Type
- protein
- Length
- 593 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription attenuation protein mtrb; Tryptophan RNA-binding attenuator…
- UniProt
- Q9X6J6, O31466
- Ligands
- TRP, ZN
- Pockets
- 7 · best druggability 0.75
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription attenuation protein mtrb | protein | 67 | 0% helix, 63% strand | Q9X6J6 |
| B | Transcription attenuation protein mtrb | protein | 70 | 0% helix, 63% strand | Q9X6J6 |
| C, D | Transcription attenuation protein mtrb | protein | 69 | 0% helix, 61% strand | Q9X6J6 |
| E, F, G, H, I, J | Tryptophan RNA-binding attenuator protein-inhibitory protein | protein | 53 | 30% helix, 19% strand | O31466 |
Ligands and binding sites
- TRP · Tryptophan · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 6 copies · chains E, F, G, H, I, J
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 81 | 0.75 | 0.98 | 20 | TRP |
| 2 | 85 | 0.74 | 0.97 | 19 | TRP |
| 3 | 75 | 0.74 | 0.98 | 19 | TRP |
| 4 | 285 | 0.62 | 0.80 | 32 | empty |
| 5 | 291 | 0.60 | 0.79 | 34 | empty |
Interfaces
21 interfaces between chains.
- B–C · 1099 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1083 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1077 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 717 Ų buried · 9 hydrogen bonds · protein-protein
- H–I · 708 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 Q9X6J6
- Every structure of UniProt O31466
- Elsewhere: RCSB PDB 2ZP8 · PDBe 2ZP8 · UniProt Q9X6J6 · UniProt O31466
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