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Crystal structures of fms1 in complex with its inhibitors
Analyse Crystal structures of fms1 in complex with its inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BI4
- Type
- protein
- Length
- 993 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Saccharomyces cerevisiae
- Molecule
- Polyamine oxidase FMS1
- EC
- 1.5.3.11
- UniProt
- P50264
- Ligands
- FAD, 298
- Pockets
- 8 · best druggability 0.87
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyamine oxidase FMS1 (EC 1.5.3.11) | protein | 497 | 37% helix, 21% strand | P50264 |
| B | Polyamine oxidase FMS1 (EC 1.5.3.11) | protein | 496 | 37% helix, 20% strand | P50264 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- 298 · N-[(1E,2Z)-but-2-en-1-ylidene]-N'-[(2E)-but-2-en-1-ylidene]butane-1,4-diamine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 601 | 0.87 | 0.92 | 91 | FAD, 298 |
| 2 | 451 | 0.86 | 0.93 | 76 | FAD, 298 |
| 3 | 179 | 0.48 | 0.76 | 28 | empty |
| 4 | 145 | 0.45 | 0.76 | 24 | empty |
| 5 | 76 | 0.43 | 0.80 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1546 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (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 3BI4 · PDBe 3BI4 · UniProt P50264
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