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Crystal structure of LSD1
Analyse Crystal structure of LSD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HKO
- Type
- protein
- Length
- 647 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine-specific histone demethylase 1
- EC
- 1.-.-.-
- UniProt
- O60341
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine-specific histone demethylase 1 (EC 1.-.-.-) | protein | 647 | 43% helix, 17% strand | O60341 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.81 | 0.82 | 99 | FAD |
| 2 | 326 | 0.61 | 0.78 | 34 | empty |
| 3 | 103 | 0.46 | 0.79 | 19 | empty |
| 4 | 128 | 0.41 | 0.75 | 20 | empty |
| 5 | 70 | 0.37 | 0.78 | 18 | empty |
Compared structures
- 2HKO · Crystal structure of LSD1 · 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 O60341
- Elsewhere: RCSB PDB 2HKO · PDBe 2HKO · UniProt O60341
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