MolNFT v1 · #186631 · protein
Estrogen receptor alpha ligand binding domain Y537S in complex with 4- (((2-chloro-5-PHENYLTHIENO[2,3-D]PYRIMIDIN-4-YL)AMINO)METHYL)PHENOL and grip peptide
7RKE: “Estrogen receptor alpha ligand binding domain Y537S in complex with 4…”. X-ray diffraction, 1 ligand (5VP), 7 pockets (best druggability 0.84). MolNFT v1 #186631 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7RKE
- Type
- protein
- Length
- 466 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen receptor; Nuclear receptor coactivator 2
- UniProt
- P03372, E7EWM1
- Ligands
- 5VP
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen receptor | protein | 220 | 71% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 229 | 68% helix, 4% strand | P03372 |
| C | Nuclear receptor coactivator 2 | protein | 7 | 71% helix, 0% strand | E7EWM1 |
| D | Nuclear receptor coactivator 2 | protein | 10 | 50% helix, 0% strand | E7EWM1 |
Ligands and binding sites
- 5VP · 4-{[(2-chloro-5-phenylthieno[2,3-d]pyrimidin-4-yl) amino]methyl}phenol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.84 | 0.97 | 23 | 5VP |
| 2 | 213 | 0.83 | 0.96 | 24 | 5VP |
| 3 | 82 | 0.57 | 0.87 | 18 | empty |
| 4 | 89 | 0.56 | 0.85 | 17 | empty |
| 5 | 248 | 0.55 | 0.77 | 37 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1529 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 547 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 455 Ų buried · 2 hydrogen bonds · protein-protein
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 E7EWM1
- Elsewhere: RCSB PDB 7RKE · PDBe 7RKE · UniProt P03372 · UniProt E7EWM1
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