MolNFT v1 · #105197 · protein
Crystal structure of histone demethylase KDM2A-H3K36ME1 with nog
4QXH · Lysine-specific demethylase 2A: “Crystal structure of histone demethylase KDM2A-H3K36ME1 with nog”. X-ray diffraction, 2 ligands (OGA, NI), 12 pockets (best druggability 0.78). MolNFT v1 #105197 on GenesisL1: 3D structure, binding…
- PDB
- 4QXH
- Type
- protein
- Length
- 817 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine-specific demethylase 2A; Histone H3.2
- EC
- 1.14.11.27
- UniProt
- F6YRW4, P84228
- Ligands
- OGA, NI
- Pockets
- 12 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Lysine-specific demethylase 2A (EC 1.14.11.27) | protein | 329 | 38% helix, 23% strand | F6YRW4 |
| B, D | Lysine-specific demethylase 2A (EC 1.14.11.27) | protein | 68 | 50% helix, 1% strand | F6YRW4 |
| E | Histone H3.2 | protein | 13 | 0% helix, 8% strand | P84228 |
| F | Histone H3.2 | protein | 10 | 0% helix, 10% strand | P84228 |
Ligands and binding sites
- OGA · N-oxalylglycine · ligand · 2 copies · chains A, E, C, F
- NI · Nickel (II) ion · metal · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 106 | 0.78 | 0.97 | 30 | OGA, NI |
| 2 | 110 | 0.71 | 0.92 | 23 | empty |
| 3 | 50 | 0.71 | 0.99 | 16 | OGA, NI |
| 4 | 836 | 0.67 | 0.74 | 61 | empty |
| 5 | 206 | 0.56 | 0.79 | 38 | empty |
Interfaces
7 interfaces between chains.
- C–D · 2049 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 2034 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 1034 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 866 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 255 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
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 F6YRW4
- Every structure of UniProt P84228
- Elsewhere: RCSB PDB 4QXH · PDBe 4QXH · UniProt F6YRW4 · UniProt P84228
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