MolNFT v1 · #18111 · protein
Structural basis for the product specificity of histone lysine methyltransferases
1PEG: “Structural basis for the product specificity of histone lysine methyltransferases”. X-ray diffraction. MolNFT v1 #18111 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PEG
- Type
- protein
- Length
- 536 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8X225, P02303
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 267 | — | Q8X225 |
| P | — | protein | 7 | — | P02303 |
| B | — | protein | 257 | — | Q8X225 |
| Q | — | protein | 5 | — | P02303 |
Compared structures
- 1PEG · Structural basis for the product specificity of histone lysine methyltransferases · the same entry in another collection · chain P against P, TM-score 1.00
- Q8X225 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase, H3 lysine-9… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q8X225
- Every structure of UniProt P02303
- Elsewhere: RCSB PDB 1PEG · PDBe 1PEG · UniProt Q8X225 · UniProt P02303
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