Research workbench
Structural insights into lysine multiple methylation by set domain methyltransferases, SET8-Y334F / H4-LYS20 / adohcy
Analyse Structural insights into lysine multiple methylation by set domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F9W
- Type
- protein
- Length
- 679 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9NQR1, P62805
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 161 | — | Q9NQR1 |
| D | — | protein | 162 | — | Q9NQR1 |
| E, G | — | protein | 9 | — | P62805 |
| F, H | — | protein | 8 | — | P62805 |
Compared structures
- 3F9W · Structural Insights into Lysine Multiple Methylation by SET Domain Methyltransferases… · the same entry in another collection · chain E against E, TM-score 1.00
- Q9NQR1 · AlphaFold monomer V2.0 prediction for N-lysine methyltransferase KMT5A (Q9NQR1) · 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 Q9NQR1
- Every structure of UniProt P62805
- Elsewhere: RCSB PDB 3F9W · PDBe 3F9W · UniProt Q9NQR1 · UniProt P62805
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