Research workbench
Crystal structure of rfxank
Analyse Crystal structure of rfxank in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UXG
- Type
- protein
- Length
- 179 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-binding protein rfxank; Histone deacetylase 4
- EC
- 3.5.1.98
- UniProt
- O14593, P56524
- Ligands
- UNX
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-binding protein rfxank | protein | 163 | 53% helix, 0% strand | O14593 |
| B | Histone deacetylase 4 (EC 3.5.1.98) | protein | 16 | 0% helix, 0% strand | P56524 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 864 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3UXG · Crystal structure of RFXANK · the same entry in another collection · chain A against A, TM-score 1.00
- O14593 · AlphaFold monomer V2.0 prediction for DNA-binding protein rfxank (O14593) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P56524 · AlphaFold monomer V2.0 prediction for histone deacetylase 4 (P56524) · a predicted model of the same protein · chain B against A, TM-score 0.23
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 O14593
- Every structure of UniProt P56524
- Elsewhere: RCSB PDB 3UXG · PDBe 3UXG · UniProt O14593 · UniProt P56524
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