Research workbench
Pandda analysis group deposition -- crystal structure of phip in complex with Z285642082
Analyse Pandda analysis group deposition -- crystal structure of phip in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5RJS
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PH-interacting protein
- UniProt
- Q8WWQ0
- Ligands
- UUP
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PH-interacting protein | protein | 119 | 69% helix, 0% strand | Q8WWQ0 |
Ligands and binding sites
- UUP · N-cyclopropylpyrazolo[1,5-a]pyrimidine-3-carboxamide · ligand · 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 | 100 | 0.51 | 0.82 | 22 | UUP |
Compared structures
- 5RJS · PanDDA analysis group deposition -- Crystal Structure of PHIP in complex with Z285642082 · 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 Q8WWQ0
- Elsewhere: RCSB PDB 5RJS · PDBe 5RJS · UniProt Q8WWQ0
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