Research workbench
Human euchromatic histone methyltransferase 1
Analyse Human euchromatic histone methyltransferase 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IGQ
- Type
- protein
- Length
- 505 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Euchromatic histone methyltransferase 1
- EC
- 2.1.1.43
- UniProt
- Q9H9B1
- Ligands
- SAH, ZN
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Euchromatic histone methyltransferase 1 (EC 2.1.1.43) | protein | 251 | 11% helix, 27% strand | Q9H9B1 |
| B | Euchromatic histone methyltransferase 1 (EC 2.1.1.43) | protein | 254 | 10% helix, 24% strand | Q9H9B1 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · 2 copies · chains A, B
- 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.80 | 0.82 | 80 | empty |
| 2 | 347 | 0.61 | 0.78 | 48 | SAH |
| 3 | 146 | 0.47 | 0.77 | 20 | SAH |
| 4 | 72 | 0.46 | 0.82 | 16 | empty |
| 5 | 124 | 0.44 | 0.77 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1086 Ų buried · 16 hydrogen bonds · protein-protein
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 Q9H9B1
- Elsewhere: RCSB PDB 2IGQ · PDBe 2IGQ · UniProt Q9H9B1
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