Research workbench
Crystal structure of SUVH9
Analyse Crystal structure of SUVH9 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4NJ5
- Type
- protein
- Length
- 482 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH9
- EC
- 2.1.1.43
- UniProt
- Q9T0G7
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH9 (EC 2.1.1.43) | protein | 482 | 22% helix, 23% strand | Q9T0G7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.55 | 0.79 | 37 | empty |
| 2 | 162 | 0.50 | 0.78 | 29 | empty |
| 3 | 104 | 0.49 | 0.81 | 21 | empty |
| 4 | 116 | 0.49 | 0.80 | 20 | empty |
| 5 | 54 | 0.39 | 0.81 | 17 | empty |
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 Q9T0G7
- Elsewhere: RCSB PDB 4NJ5 · PDBe 4NJ5 · UniProt Q9T0G7
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