MolNFT v1 · #28719 · protein
Mouse sf-1 lbd
1YMT · Steroidogenic factor 1: “Mouse sf-1 lbd”. X-ray diffraction, 1 ligand (DR9), 2 pockets (best druggability 0.84). MolNFT v1 #28719 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1YMT
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Steroidogenic factor 1; Nuclear receptor 0B2
- UniProt
- P33242, Q62227
- Ligands
- DR9
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Steroidogenic factor 1 | protein | 235 | 72% helix, 3% strand | P33242 |
| B | Nuclear receptor 0B2 | protein | 10 | 60% helix, 0% strand | Q62227 |
Ligands and binding sites
- DR9 · 1-cis-9-octadecanoyl-2-cis-9-hexadecanoyl phosphatidyl glycerol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 577 | 0.84 | 0.89 | 47 | DR9 |
| 2 | 87 | 0.63 | 0.90 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 481 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1YMT · Mouse SF-1 LBD · the same entry in another collection · chain A against A, TM-score 1.00
- P33242 · AlphaFold monomer V2.0 prediction for steroidogenic factor 1 (P33242) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q62227 · AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 0 group B member 2… · a predicted model of the same protein · chain B against A, TM-score 0.71
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 P33242
- Every structure of UniProt Q62227
- Elsewhere: RCSB PDB 1YMT · PDBe 1YMT · UniProt P33242 · UniProt Q62227
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