Research workbench
Crystal structure of P. aeruginosa ohr
Analyse Crystal structure of P. aeruginosa ohr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N2F
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Organic hydroperoxide resistance protein
- UniProt
- Q9HZZ3
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Organic hydroperoxide resistance protein | protein | 142 | 33% helix, 35% strand | Q9HZZ3 |
Ligands and binding sites
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.46 | 0.79 | 16 | DTT |
| 2 | 111 | 0.46 | 0.78 | 18 | DTT |
Interfaces
1 interface between chains.
- A–B · 3342 Ų buried · 52 hydrogen bonds · protein-protein
Compared structures
- 1N2F · Crystal structure of P. aeruginosa ohr · 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 Q9HZZ3
- Elsewhere: RCSB PDB 1N2F · PDBe 1N2F · UniProt Q9HZZ3
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