MolNFT v1 · #51233 · protein
Structural basis of LSD1-corest selectivity in histone H3 recognition
2V1D: “Structural basis of LSD1-corest selectivity in histone H3 recognition”. X-ray diffraction. MolNFT v1 #51233 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2V1D
- Type
- protein
- Length
- 815 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60341, Q9UKL0, Q16695
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 666 | — | O60341 |
| B | — | protein | 133 | — | Q9UKL0 |
| C | — | protein | 16 | — | Q16695 |
Compared structures
- 2V1D · Structural basis of LSD1-CoREST selectivity in histone H3 recognition · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UKL0 · AlphaFold monomer V2.0 prediction for rest corepressor 1 (Q9UKL0) · a predicted model of the same protein · chain B against A, TM-score 0.98
- Q16695 · AlphaFold monomer V2.0 prediction for histone H3.1T (Q16695) · a predicted model of the same protein · chain C against A, TM-score 0.25
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 O60341
- Every structure of UniProt Q9UKL0
- Every structure of UniProt Q16695
- Elsewhere: RCSB PDB 2V1D · PDBe 2V1D · UniProt O60341 · UniProt Q9UKL0 · UniProt Q16695
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