MolNFT v1 · #133056 · protein
Pandda analysis group deposition -- crystal structure of phip in complex with Z53116498
5RK8 · PH-interacting protein: “Pandda analysis group deposition -- crystal structure of phip in complex with Z53116498”. X-ray diffraction, 1 ligand (UVJ), 1 pocket (best druggability 0.54). MolNFT v1 #133056 on GenesisL1: 3D structure…
- PDB
- 5RK8
- 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
- UVJ
- Pockets
- 1 · best druggability 0.54
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
- UVJ · 3-(2-methyl-1H-benzimidazol-1-yl)propanamide · 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 | 117 | 0.54 | 0.82 | 22 | UVJ |
Compared structures
- 5RK8 · PanDDA analysis group deposition -- Crystal Structure of PHIP in complex with Z53116498 · 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 5RK8 · PDBe 5RK8 · UniProt Q8WWQ0
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