Research workbench
Structure-activity relationship studies of allosteric inhibitors of EYA2 tyrosine phosphatase
Analyse Structure-activity relationship studies of allosteric inhibitors of EYA2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F8H
- Type
- protein
- Length
- 778 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O00167
- Ligands
- 1SI
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 257 | — | O00167 |
| A | — | protein | 259 | — | O00167 |
| C | — | protein | 262 | — | O00167 |
Ligands and binding sites
- 1SI · 3-fluoranyl-~{N}-[(~{E})-(5-pyridin-2-ylsulfanylfuran-2-yl)methylideneamino]benzamide · ligand · 3 copies · chains B, A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7F8H · Structure-activity relationship studies of allosteric inhibitors of EYA2 tyrosine… · the same entry in another collection · chain B against B, TM-score 1.00
- O00167 · AlphaFold monomer V2.0 prediction for eyes absent homolog 2 (O00167) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O00167
- Elsewhere: RCSB PDB 7F8H · PDBe 7F8H · UniProt O00167
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