Research workbench
Dcoh, a bifunctional protein-binding transcriptional coactivator, PRO9LEU mutant
Analyse Dcoh, a bifunctional protein-binding transcriptional coactivator, PRO9LEU mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1USO
- Type
- protein
- Length
- 155 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte nuclear factor 1-alpha
- Ligands
- SO4
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte nuclear factor 1-alpha | protein | 77 | 38% helix, 30% strand | — |
| B | Hepatocyte nuclear factor 1-alpha | protein | 78 | 40% helix, 29% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 735 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1USO · Dcoh, a bifunctional protein-binding transcriptional coactivator, PRO9LEU mutant · 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
- Elsewhere: RCSB PDB 1USO · PDBe 1USO
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