Research workbench
Structure of coenzyme F420H2:NADP+ oxidoreductase (fno)
Analyse Structure of coenzyme F420H2:NADP+ oxidoreductase (fno) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JAX
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Conserved hypothetical protein
- UniProt
- O29370
- Ligands
- NA, MG
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Conserved hypothetical protein | protein | 212 | 44% helix, 25% strand | O29370 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 302 | 0.58 | 0.77 | 29 | empty |
| 2 | 272 | 0.56 | 0.77 | 27 | empty |
| 3 | 54 | 0.33 | 0.78 | 16 | empty |
| 4 | 50 | 0.28 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1463 Ų buried · 30 hydrogen bonds · protein-protein
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 O29370
- Elsewhere: RCSB PDB 1JAX · PDBe 1JAX · UniProt O29370
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