Research workbench
Complexe of arno SEC7 domain with the protein-protein interaction inhibitor N-(4-hydroxy-2,6-DIMETHYLPHENYL)BENZENESULFONAMIDE at PH6.5
Analyse Complexe of arno SEC7 domain with the protein-protein interaction inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L5M
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytohesin-2
- UniProt
- Q99418
- Ligands
- HRC, PO4
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 65% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytohesin-2 | protein | 196 | 65% helix, 1% strand | Q99418 |
Ligands and binding sites
- HRC · N-(4-hydroxy-2,6-dimethylphenyl)benzenesulfonamide · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.52 | 0.79 | 17 | HRC |
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 Q99418
- Elsewhere: RCSB PDB 4L5M · PDBe 4L5M · UniProt Q99418
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