MolNFT v1 · #187914 · protein
Estrogen receptor alpha ligand binding domain Y537S in complex with 2- chloro-4-((4-HYDROXYBENZYL)AMINO)-5-PHENYLTHIENO[2,3-D]PYRIMIDIN-6-ol and grip peptide
7T2X: “Estrogen receptor alpha ligand binding domain Y537S in complex with 2…”. X-ray diffraction, 1 ligand (EMY), 7 pockets (best druggability 0.84). MolNFT v1 #187914 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7T2X
- Type
- protein
- Length
- 455 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
- EMY
- 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 | 210 | 70% helix, 4% strand | P03372 |
| B | Estrogen receptor | protein | 227 | 69% helix, 4% strand | P03372 |
| C | Nuclear receptor coactivator 2 | protein | 8 | 75% helix, 0% strand | Q15596 |
| D | Nuclear receptor coactivator 2 | protein | 10 | 50% helix, 0% strand | Q15596 |
Ligands and binding sites
- EMY · S-(2-chloro-6-{[(4-hydroxyphenyl) methyl]amino}pyrimidin-4-yl) phenylethanethioate · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 194 | 0.84 | 0.97 | 25 | EMY |
| 2 | 280 | 0.83 | 0.93 | 26 | EMY |
| 3 | 73 | 0.59 | 0.89 | 19 | empty |
| 4 | 71 | 0.54 | 0.87 | 18 | empty |
| 5 | 71 | 0.53 | 0.86 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1524 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 513 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 404 Ų buried · 0 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 Q15596
- Elsewhere: RCSB PDB 7T2X · PDBe 7T2X · UniProt P03372 · UniProt Q15596
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