Research workbench
Crystal structure of HNF4A lbd in complex with the ligand and the coactivator src-1 peptide
Analyse Crystal structure of HNF4A lbd in complex with the ligand and the coactivator… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PZL
- Type
- protein
- Length
- 241 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hepatocyte nuclear factor 4-alpha; Steroid receptor coactivator-1
- UniProt
- P41235
- Ligands
- MYR
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hepatocyte nuclear factor 4-alpha | protein | 227 | 67% helix, 3% strand | P41235 |
| B | Steroid receptor coactivator-1 | protein | 14 | 64% helix, 0% strand | — |
Ligands and binding sites
- MYR · Myristic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 261 | 0.83 | 0.94 | 40 | MYR |
| 2 | 82 | 0.34 | 0.75 | 23 | empty |
| 3 | 67 | 0.34 | 0.76 | 18 | empty |
| 4 | 64 | 0.32 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 572 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1PZL · Crystal structure of HNF4a LBD in complex with the ligand and the coactivator SRC-1… · the same entry in another collection · chain A against A, TM-score 1.00
- P41235 · AlphaFold monomer V2.0 prediction for hepatocyte nuclear factor 4-alpha (P41235) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P41235
- Elsewhere: RCSB PDB 1PZL · PDBe 1PZL · UniProt P41235
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