MolNFT v1 · #71136 · protein
SET7/9 in complex with TAF10 peptide and adohcy
3M53 · Histone-lysine N-methyltransferase SETD7: “SET7/9 in complex with TAF10 peptide and adohcy”. X-ray diffraction, 2 ligands (ACE, SAH), 1 pocket (best druggability 0.47). MolNFT v1 #71136 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3M53
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase SETD7; TAF10 peptide
- EC
- 2.1.1.43
- UniProt
- Q8WTS6
- Ligands
- ACE, SAH
- Pockets
- 1 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) | protein | 246 | 11% helix, 38% strand | Q8WTS6 |
| B | TAF10 peptide | protein | 8 | 0% helix, 13% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 180 | 0.47 | 0.75 | 28 | SAH |
Interfaces
1 interface between chains.
- A–B · 689 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 Q8WTS6
- Elsewhere: RCSB PDB 3M53 · PDBe 3M53 · UniProt Q8WTS6
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