Research workbench
Complex structure of atrx add domain bound to unmodified H3 1-15 peptide
Analyse Complex structure of atrx add domain bound to unmodified H3 1-15 peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QLC
- Type
- protein
- Length
- 268 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46100, P84243
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 127 | — | P46100 |
| C, D | — | protein | 7 | — | P84243 |
Compared structures
- 3QLC · Complex structure of ATRX ADD domain bound to unmodified H3 1-15 peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P46100 · AlphaFold monomer V2.0 prediction for transcriptional regulator atrx (P46100) · a predicted model of the same protein · chain B against A, TM-score 0.94
- P84243 · AlphaFold monomer V2.0 prediction for histone H3.3 (P84243) · a predicted model of the same protein · chain C against A, TM-score 0.53
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 P46100
- Every structure of UniProt P84243
- Elsewhere: RCSB PDB 3QLC · PDBe 3QLC · UniProt P46100 · UniProt P84243
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