Research workbench
Crystal structure of the human NUR77 ligand-binding domain
Analyse Crystal structure of the human NUR77 ligand-binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V3E
- Type
- protein
- Length
- 471 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear receptor subfamily 4 group a member 1
- UniProt
- P22736
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Nuclear receptor subfamily 4 group a member 1 | protein | 237 | 68% helix, 4% strand | P22736 |
| A | Nuclear receptor subfamily 4 group a member 1 | protein | 234 | 67% helix, 4% strand | P22736 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 410 | 0.60 | 0.76 | 49 | empty |
| 2 | 141 | 0.60 | 0.83 | 21 | GOL |
| 3 | 142 | 0.44 | 0.76 | 18 | empty |
| 4 | 95 | 0.41 | 0.77 | 16 | GOL |
| 5 | 103 | 0.40 | 0.76 | 16 | GOL |
Interfaces
1 interface between chains.
- B–A · 608 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3V3E · Crystal Structure of the Human Nur77 Ligand-binding Domain · the same entry in another collection · chain B against B, TM-score 1.00
- P22736 · AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 4 group a member 1… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P22736
- Elsewhere: RCSB PDB 3V3E · PDBe 3V3E · UniProt P22736
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