Research workbench
Discovery of fragment-inspired heterocyclic benzenesulfonmides as inhibitors of the WDR5-myc interaction
Analyse Discovery of fragment-inspired heterocyclic benzenesulfonmides as inhibitors of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UIF
- Type
- protein
- Length
- 601 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P61964
- Ligands
- Q8P
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 301 | — | P61964 |
| B | — | protein | 300 | — | P61964 |
Ligands and binding sites
- Q8P · 4-{[(5-bromo-3-chloro-2-hydroxyphenyl)sulfonyl]amino}-1-cyclopentyl-N-methyl-1H-imidazole-2-carboxamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UIF · Discovery of fragment-inspired heterocyclic benzenesulfonmides as inhibitors of the… · 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 P61964
- Elsewhere: RCSB PDB 6UIF · PDBe 6UIF · UniProt P61964
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