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Structure of the dirigent protein DRR206
Analyse Structure of the dirigent protein DRR206 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4REV
- Type
- protein
- Length
- 255 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disease resistance response protein 206
- UniProt
- P13240
- Ligands
- DMI, CL
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disease resistance response protein 206 | protein | 128 | 0% helix, 64% strand | P13240 |
| B | Disease resistance response protein 206 | protein | 127 | 0% helix, 63% strand | P13240 |
Ligands and binding sites
- DMI · 2,3-dimethylimidazolium ion · ligand · chains B
- CL · Chloride ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.62 | 0.80 | 24 | empty |
| 2 | 250 | 0.58 | 0.78 | 23 | empty |
| 3 | 202 | 0.55 | 0.78 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 392 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P13240
- Elsewhere: RCSB PDB 4REV · PDBe 4REV · UniProt P13240
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