Research workbench
Crystal structure of scribble PDZ34 tandem at 2.6 ångströms
Analyse Crystal structure of scribble PDZ34 tandem at 2.6 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WYT
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein scribble homolog
- UniProt
- Q14160
- Ligands
- CL
- Pockets
- 3 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein scribble homolog | protein | 201 | 13% helix, 30% strand | Q14160 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 66 | 0.33 | 0.76 | 11 | CL |
| 2 | 55 | 0.30 | 0.76 | 20 | empty |
| 3 | 57 | 0.29 | 0.74 | 15 | empty |
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 Q14160
- Elsewhere: RCSB PDB 4WYT · PDBe 4WYT · UniProt Q14160
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