Research workbench
Structures of the apo-and metal ion activated forms of the diphtheria tox repressor from corynebacterium diphtheriae
Analyse Structures of the apo-and metal ion activated forms of the diphtheria tox… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DPR
- Type
- protein
- Length
- 268 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diphtheria tox repressor
- UniProt
- P33120
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Diphtheria tox repressor | protein | 134 | 58% helix, 3% strand | P33120 |
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 | 91 | 0.31 | 0.72 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 891 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1DPR · Structures of the apo-and metal ion activated forms of the diphtheria tox repressor from… · 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
- Every structure of UniProt P33120
- Elsewhere: RCSB PDB 1DPR · PDBe 1DPR · UniProt P33120
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.