Research workbench
Ohra (organic hydroperoxide resistance protein) wild type from chromobacterium violaceum
Analyse Ohra (organic hydroperoxide resistance protein) wild type from chromobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ECY
- Type
- protein
- Length
- 298 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Organic hydroperoxide resistance protein
- UniProt
- Q7P1K4
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Organic hydroperoxide resistance protein | protein | 143 | 33% helix, 29% strand | Q7P1K4 |
| B | Organic hydroperoxide resistance protein | protein | 155 | 30% helix, 26% strand | Q7P1K4 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.68 | 0.83 | 33 | empty |
| 2 | 221 | 0.66 | 0.84 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 3380 Ų buried · 58 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6ECY · OhrA (Organic Hydroperoxide Resistance protein) wild type from chromobacterium violaceum · 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 Q7P1K4
- Elsewhere: RCSB PDB 6ECY · PDBe 6ECY · UniProt Q7P1K4
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