Research workbench
Crystal structure of the TRP RNA-binding attenuation protein (trap) from bacillus licheniformis.
Analyse Crystal structure of the TRP RNA-binding attenuation protein (trap) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZTE
- Type
- protein
- Length
- 1,500 residues
- Chains
- 22
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan operon RNA-binding attenuation protein (trap)
- UniProt
- Q65I22
- Ligands
- TRP
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 0% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, K, M, N, O, P, Q, R, S, T, V | Tryptophan operon RNA-binding attenuation protein (trap) | protein | 68 | 0% helix, 62% strand | Q65I22 |
| J, U | Tryptophan operon RNA-binding attenuation protein (trap) | protein | 69 | 0% helix, 61% strand | Q65I22 |
| L | Tryptophan operon RNA-binding attenuation protein (trap) | protein | 70 | 0% helix, 60% strand | Q65I22 |
Ligands and binding sites
- TRP · Tryptophan · ligand · 22 copies · chains A, K, B, C, D, E, F, G, H, I, J, L, V, M, N, O, P, Q, R, S, T, U
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 451 | 0.79 | 0.87 | 68 | empty |
| 2 | 77 | 0.75 | 0.98 | 20 | TRP |
| 3 | 78 | 0.75 | 0.98 | 22 | TRP |
| 4 | 77 | 0.74 | 0.98 | 21 | TRP |
| 5 | 88 | 0.74 | 0.97 | 22 | TRP |
Interfaces
42 interfaces between chains.
- Q–R · 1117 Ų buried · 18 hydrogen bonds · protein-protein
- F–G · 1108 Ų buried · 16 hydrogen bonds · protein-protein
- O–P · 1100 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 1097 Ų buried · 19 hydrogen bonds · protein-protein
- L–V · 1095 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3ZTE · Crystal Structure of the TRP RNA-Binding Attenuation Protein (TRAP) from Bacillus… · the same entry in another collection · chain B against B, 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 Q65I22
- Elsewhere: RCSB PDB 3ZTE · PDBe 3ZTE · UniProt Q65I22
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