Research workbench
Crystal structure of human scribble PDZ1:VANGL2 complex
Analyse Crystal structure of human scribble PDZ1:VANGL2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6XA8
- Type
- protein
- Length
- 218 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein scribble homolog; C-terminal peptide of VANGL2
- UniProt
- Q14160
- Ligands
- PO4
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein scribble homolog | protein | 102 | 14% helix, 41% strand | Q14160 |
| C, D | C-terminal peptide of VANGL2 | protein | 7 | 0% helix, 43% strand | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, D, B
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 806 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 473 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 469 Ų buried · 13 hydrogen bonds · protein-protein
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 6XA8 · PDBe 6XA8 · UniProt Q14160
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