MolNFT v1 · #59114 · protein
Crystal structure of methyltransferase domain of human histone-lysine N-methyltransferase setmar
3BO5: “Crystal structure of methyltransferase domain of human histone-lysine N-methyltransferase setmar”. X-ray diffraction, 2 ligands (SAH, ZN), 4 pockets (best druggability 0.64). MolNFT v1 #59114 on GenesisL1: 3D structure, binding…
- PDB
- 3BO5
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase setmar
- EC
- 2.1.1.43
- UniProt
- Q53H47
- Ligands
- SAH, ZN
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase setmar (EC 2.1.1.43) | protein | 269 | 7% helix, 29% strand | Q53H47 |
Ligands and binding sites
- SAH · S-adenosyl-L-homocysteine · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 276 | 0.64 | 0.81 | 37 | SAH |
| 2 | 335 | 0.60 | 0.77 | 45 | empty |
| 3 | 61 | 0.40 | 0.80 | 16 | empty |
| 4 | 101 | 0.39 | 0.76 | 29 | empty |
Compared structures
- 3BO5 · Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q53H47 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase setmar (Q53H47) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q53H47
- Elsewhere: RCSB PDB 3BO5 · PDBe 3BO5 · UniProt Q53H47
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