Research workbench
The structure of anti-trap
Analyse The structure of anti-trap in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KO8
- Type
- protein
- Length
- 159 residues
- Chains
- 3
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryptophan RNA-binding attenuator protein inhibitory protein
- UniProt
- O31466
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.37
Structure
solution nmr · 1 distinct chain · 34% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Tryptophan RNA-binding attenuator protein inhibitory protein | protein | 53 | 34% helix, 11% strand | O31466 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.37 | 0.76 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–C · 635 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 631 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 631 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (formylation).
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 O31466
- Elsewhere: RCSB PDB 2KO8 · PDBe 2KO8 · UniProt O31466
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