MolNFT v1 · #31657 · protein
Human estrogen receptor alpha ligand-binding domain in complex with 17METHYL-17ALPHA-dihydroequilenin and a glucoc interacting protein 1 nr box II peptide
2B1Z: “Human estrogen receptor alpha ligand-binding domain in complex with 17METHYL-17ALPHA-dihydroequilenin and a…”. X-ray diffraction, 1 ligand (17M), 6 pockets (best druggability 0.85). MolNFT v1 #31657 on GenesisL1: 3D structure…
- PDB
- 2B1Z
- Type
- protein
- Length
- 490 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Nuclear receptor coactivator 2
- UniProt
- P03372, Q15596
- Ligands
- 17M
- Pockets
- 6 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 235 | 70% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 238 | 68% helix, 4% strand | P03372 |
| C | Nuclear receptor coactivator 2 | protein | 8 | 75% helix, 0% strand | Q15596 |
| D | Nuclear receptor coactivator 2 | protein | 9 | 78% helix, 0% strand | Q15596 |
Ligands and binding sites
- 17M · 17-methyl-17-alpha-dihydroequilenin · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.85 | 0.98 | 22 | 17M |
| 2 | 183 | 0.84 | 0.98 | 21 | 17M |
| 3 | 102 | 0.63 | 0.88 | 22 | empty |
| 4 | 97 | 0.61 | 0.88 | 21 | empty |
| 5 | 242 | 0.55 | 0.77 | 30 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1879 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 516 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 506 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (artifact).
Compared structures
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 P03372
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 2B1Z · PDBe 2B1Z · UniProt P03372 · UniProt Q15596
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