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Crystal structure of human scribble PDZ1:MCC complex
Analyse Crystal structure of human scribble PDZ1:MCC complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MTV
- Type
- protein
- Length
- 209 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein scribble homolog; Colorectal mutant cancer protein
- UniProt
- Q14160
- Ligands
- SO4
Structure
x-ray diffraction · 4 distinct chains · 13% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein scribble homolog | protein | 98 | 14% helix, 39% strand | Q14160 |
| B | Protein scribble homolog | protein | 99 | 13% helix, 34% strand | Q14160 |
| D | Colorectal mutant cancer protein | protein | 7 | 0% helix, 43% strand | — |
| E | Colorectal mutant cancer protein | protein | 5 | 0% helix, 40% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 495 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 439 Ų buried · 13 hydrogen bonds · protein-protein
- B–E · 325 Ų buried · 6 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 6MTV · PDBe 6MTV · UniProt Q14160
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