Research workbench
Structure of histone demethylase REF6 at 1.8A
Analyse Structure of histone demethylase REF6 at 1.8A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A59
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine-specific demethylase REF6
- EC
- 1.14.11.-
- UniProt
- Q9STM3
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine-specific demethylase REF6 (EC 1.14.11.-) | protein | 114 | 36% helix, 12% strand | Q9STM3 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q9STM3
- Elsewhere: RCSB PDB 6A59 · PDBe 6A59 · UniProt Q9STM3
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