MolNFT v1 · #108729 · protein
Crystal structure of a tridecameric superhelix
4WG0 · Nuclear receptor coactivator 2: “Crystal structure of a tridecameric superhelix”. X-ray diffraction, 4 ligands (ACE, CHD, SO4), 6 pockets (best druggability 0.39). MolNFT v1 #108729 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4WG0
- Type
- protein
- Length
- 169 residues
- Chains
- 13
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclear receptor coactivator 2
- UniProt
- Q15596
- Ligands
- ACE, CHD, SO4, NH2
- Pockets
- 6 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M | Nuclear receptor coactivator 2 | protein | 13 | 69% helix, 0% strand | Q15596 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 13 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M
- CHD · Cholic acid · ligand · 13 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M
- SO4 · Sulfate ion · ion · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M
- NH2 · Amino group · ion · 13 copies · chains A, B, E, D, G, C, F, I, H, K, J, M, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.39 | 0.73 | 18 | CHD |
| 2 | 124 | 0.37 | 0.73 | 18 | CHD |
| 3 | 111 | 0.36 | 0.73 | 17 | CHD |
| 4 | 115 | 0.36 | 0.73 | 18 | CHD |
| 5 | 64 | 0.28 | 0.73 | 11 | CHD |
Interfaces
33 interfaces between chains.
- D–E · 322 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 319 Ų buried · 2 hydrogen bonds · protein-protein
- F–G · 319 Ų buried · 3 hydrogen bonds · protein-protein
- L–M · 317 Ų buried · 2 hydrogen bonds · protein-protein
- H–I · 317 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 covalent (covalent ligand).
Compared structures
- 4WG0 · Crystal structure of a tridecameric superhelix · 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
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 4WG0 · PDBe 4WG0 · UniProt Q15596
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