MolNFT v1 · #20864 · protein
Crystal structure of the polyamine oxidase FMS1 from yeast
1RSG · FMS1 protein: “Crystal structure of the polyamine oxidase FMS1 from yeast”. X-ray diffraction, 1 ligand (FAD), 11 pockets (best druggability 0.88). MolNFT v1 #20864 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1RSG
- Type
- protein
- Length
- 972 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMS1 protein
- EC
- 1.5.3.11
- UniProt
- P50264
- Ligands
- FAD
- Pockets
- 11 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMS1 protein (EC 1.5.3.11) | protein | 481 | 38% helix, 20% strand | P50264 |
| B | FMS1 protein (EC 1.5.3.11) | protein | 491 | 37% helix, 20% strand | P50264 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 592 | 0.88 | 0.93 | 80 | FAD |
| 2 | 525 | 0.87 | 0.93 | 84 | FAD |
| 3 | 307 | 0.62 | 0.79 | 33 | empty |
| 4 | 313 | 0.59 | 0.77 | 33 | empty |
| 5 | 283 | 0.55 | 0.76 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 1585 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified, 4 disulfide (engineered, 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 P50264
- Elsewhere: RCSB PDB 1RSG · PDBe 1RSG · UniProt P50264
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