MolNFT v1 · #49929 · protein
Methyltransferase domain of human suppressor of variegation 3-9 homolog 2
2R3A · Histone-lysine N-methyltransferase SUV39H2: “Methyltransferase domain of human suppressor of variegation 3-9 homolog 2”. X-ray diffraction, 3 ligands (SAM, SER, ZN), 4 pockets (best druggability 0.63). MolNFT v1 #49929 on GenesisL1…
- PDB
- 2R3A
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase SUV39H2
- EC
- 2.1.1.43
- UniProt
- Q9H5I1
- Ligands
- SAM, SER, ZN
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) | protein | 270 | 19% helix, 23% strand | Q9H5I1 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · chains A
- SER · Serine · ligand · chains A
- ZN · Zinc ion · metal · 4 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 | 370 | 0.63 | 0.78 | 50 | SAM |
| 2 | 125 | 0.50 | 0.80 | 30 | empty |
| 3 | 98 | 0.43 | 0.78 | 23 | empty |
| 4 | 68 | 0.36 | 0.77 | 15 | empty |
Compared structures
- 2R3A · Methyltransferase domain of human suppressor of variegation 3-9 homolog 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H5I1 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SUV39H2 (Q9H5I1) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9H5I1
- Elsewhere: RCSB PDB 2R3A · PDBe 2R3A · UniProt Q9H5I1
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