Research workbench
Crystal structure of JMJD2A complexed with histone H3 peptide trimethylated at LYS36
Analyse Crystal structure of JMJD2A complexed with histone H3 peptide trimethylated at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OS2
- Type
- protein
- Length
- 717 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O75164
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 347 | — | O75164 |
| B | — | protein | 348 | — | O75164 |
| C, D | — | protein | 11 | — | — |
Compared structures
- 2OS2 · Crystal structure of JMJD2A complexed with histone H3 peptide trimethylated at Lys36 · the same entry in another collection · chain A against A, TM-score 1.00
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 O75164
- Elsewhere: RCSB PDB 2OS2 · PDBe 2OS2 · UniProt O75164
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