Research workbench
Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with sah and mono-methylated H3K9 peptide
Analyse Crystal structure of catalytic domain of human euchromatic histone… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HNA
- Type
- protein
- Length
- 559 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase, H3 lysine-9 specific 5; Mono-methylated H3K9 peptide
- EC
- 2.1.1.43
- UniProt
- Q9H9B1
- Ligands
- SAH, ZN
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 12% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase, H3 lysine-9 specific 5 (EC 2.1.1.43) | protein | 280 | 14% helix, 24% strand | Q9H9B1 |
| B | Histone-lysine N-methyltransferase, H3 lysine-9 specific 5 (EC 2.1.1.43) | protein | 260 | 10% helix, 26% strand | Q9H9B1 |
| P | Mono-methylated H3K9 peptide | protein | 8 | 0% helix, 13% strand | — |
| Q | Mono-methylated H3K9 peptide | protein | 11 | 0% helix, 9% strand | — |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, P, B, Q
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.81 | 0.82 | 99 | empty |
| 2 | 150 | 0.58 | 0.83 | 23 | empty |
| 3 | 209 | 0.56 | 0.79 | 25 | SAH |
| 4 | 232 | 0.54 | 0.77 | 27 | SAH |
| 5 | 91 | 0.38 | 0.76 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1293 Ų buried · 19 hydrogen bonds · protein-protein
- B–Q · 980 Ų buried · 27 hydrogen bonds · protein-protein
- A–P · 800 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 3HNA · Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in… · the same entry in another collection · chain B against B, TM-score 1.00
- Q9H9B1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase EHMT1 (Q9H9B1) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9H9B1
- Elsewhere: RCSB PDB 3HNA · PDBe 3HNA · UniProt Q9H9B1
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