MolNFT v1 · #47289 · protein
Crystal structure of a pyridoxamine 5'-phosphate oxidase-related FMN- binding protein (JANN_0254) from jannaschia sp. CCS1 at 1.60 a resolution
2OU5 · Pyridoxamine 5'-phosphate oxidase-related, FMN-binding: “Crystal structure of a pyridoxamine 5'-phosphate oxidase-related FMN- binding protein (JANN_0254) from…”. X-ray diffraction, 2 ligands (FMN, SO4), 3 pockets (best druggability…
- PDB
- 2OU5
- Type
- protein
- Length
- 350 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyridoxamine 5'-phosphate oxidase-related, FMN-binding
- UniProt
- Q28VU1
- Ligands
- FMN, SO4
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pyridoxamine 5'-phosphate oxidase-related, FMN-binding | protein | 175 | 27% helix, 39% strand | Q28VU1 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
- GOL · Glycerol · additive · 4 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 | 701 | 0.74 | 0.80 | 60 | FMN |
| 2 | 551 | 0.71 | 0.80 | 53 | FMN, GOL |
| 3 | 229 | 0.61 | 0.81 | 25 | GOL |
Interfaces
1 interface between chains.
- A–B · 1520 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 2OU5 · Crystal structure of a pyridoxamine 5'-phosphate oxidase-related fmn-binding protein… · 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 Q28VU1
- Elsewhere: RCSB PDB 2OU5 · PDBe 2OU5 · UniProt Q28VU1
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