Research workbench
Human SETD6 in complex with rela LYS310
Analyse Human SETD6 in complex with rela LYS310 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QXY
- Type
- protein
- Length
- 836 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-lysine methyltransferase SETD6; Transcription factor P65
- EC
- 2.1.1.-
- UniProt
- Q8TBK2, Q04206
- Ligands
- SAM
- Pockets
- 14 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-lysine methyltransferase SETD6 (EC 2.1.1.-) | protein | 420 | 50% helix, 12% strand | Q8TBK2 |
| P, Q | Transcription factor P65 | protein | 1 | 0% helix, 0% strand | Q04206 |
| B | N-lysine methyltransferase SETD6 (EC 2.1.1.-) | protein | 414 | 50% helix, 13% strand | Q8TBK2 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 17 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 308 | 0.69 | 0.83 | 40 | SAM, EDO |
| 2 | 336 | 0.68 | 0.82 | 39 | SAM, EDO |
| 3 | 79 | 0.44 | 0.80 | 14 | EDO |
| 4 | 105 | 0.43 | 0.77 | 20 | EDO |
| 5 | 100 | 0.38 | 0.75 | 18 | EDO |
Interfaces
3 interfaces between chains.
- A–B · 441 Ų buried · 9 hydrogen bonds · protein-protein
- A–P · 185 Ų buried · 5 hydrogen bonds · protein-protein
- B–Q · 178 Ų buried · 5 hydrogen bonds · protein-protein
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 Q8TBK2
- Every structure of UniProt Q04206
- Elsewhere: RCSB PDB 3QXY · PDBe 3QXY · UniProt Q8TBK2 · UniProt Q04206
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