Research workbench
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
- 3BI2
- Type
- protein
- Length
- 993 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyamine oxidase FMS1
- EC
- 1.5.3.11
- UniProt
- P50264
- Ligands
- FAD, 297
- Pockets
- 8 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyamine oxidase FMS1 (EC 1.5.3.11) | protein | 494 | 36% helix, 21% strand | P50264 |
| B | Polyamine oxidase FMS1 (EC 1.5.3.11) | protein | 499 | 35% helix, 20% strand | P50264 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- 297 · dodecane-1,12-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 | 637 | 0.88 | 0.92 | 93 | FAD, 297 |
| 2 | 574 | 0.87 | 0.92 | 86 | FAD, 297 |
| 3 | 174 | 0.46 | 0.75 | 26 | empty |
| 4 | 173 | 0.44 | 0.74 | 22 | empty |
| 5 | 141 | 0.43 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1580 Ų buried · 18 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 3BI2 · PDBe 3BI2 · UniProt P50264
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