Research workbench
The molecular structure of a DNA-triostin a complex
Analyse The molecular structure of a DNA-triostin a complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VTG
- Type
- protein + DNA
- Length
- 14 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*CP*GP*TP*AP*CP*G)-3'); Triostin a
- Ligands
- QUI
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA (5'-D(*CP*GP*TP*AP*CP*G)-3') | dna | 6 | — | — |
| B | Triostin a | protein | 8 | 0% helix, 0% strand | — |
Ligands and binding sites
- QUI · 2-carboxyquinoxaline · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 187 Ų buried · 2 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 4 modified, 2 covalent, 2 d-amino (covalent ligand, D-amino acid, methylation, nonstandard).
Compared structures
- 1VTG · The molecular structure of a DNA-triostin a 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
- Elsewhere: RCSB PDB 1VTG · PDBe 1VTG
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