Research workbench
Crystal structure of arabidopsis thaliana SUVH6 in complex with SAM, form 2
Analyse Crystal structure of arabidopsis thaliana SUVH6 in complex with SAM, form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A5M
- Type
- protein
- Length
- 488 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6
- EC
- 2.1.1.43
- UniProt
- Q8VZ17
- Ligands
- SAM, ZN
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6 (EC 2.1.1.43) | protein | 488 | 20% helix, 24% strand | Q8VZ17 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 384 | 0.69 | 0.82 | 65 | empty |
| 2 | 403 | 0.68 | 0.80 | 49 | SAM |
| 3 | 460 | 0.63 | 0.77 | 62 | empty |
| 4 | 87 | 0.50 | 0.83 | 21 | empty |
| 5 | 149 | 0.45 | 0.76 | 26 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 6A5M · Crystal structure of Arabidopsis thaliana SUVH6 in complex with SAM, form 2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8VZ17 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-9… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q8VZ17
- Elsewhere: RCSB PDB 6A5M · PDBe 6A5M · UniProt Q8VZ17
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