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Crystal structure of Human LSD1
Analyse Crystal structure of Human LSD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NQM
- Type
- protein
- Length
- 636 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Homo sapiens
- Molecule
- Lysine-specific histone demethylase 1A
- EC
- 1.-.-.-
- UniProt
- O60341
- Ligands
- FAD
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · resolution 2.9 · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine-specific histone demethylase 1A (EC 1.-.-.-) | protein | 636 | 46% helix, 16% 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 | 1033 | 0.82 | 0.83 | 90 | FAD |
| 2 | 286 | 0.60 | 0.79 | 29 | empty |
| 3 | 100 | 0.44 | 0.78 | 19 | empty |
| 4 | 119 | 0.39 | 0.75 | 21 | empty |
| 5 | 69 | 0.38 | 0.79 | 21 | empty |
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 O60341
- Elsewhere: RCSB PDB 6NQM · PDBe 6NQM · UniProt O60341
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