Research workbench
PDZ domain from rat SHANK3 bound to the C terminus of PROSAPIP1
Analyse PDZ domain from rat SHANK3 bound to the C terminus of PROSAPIP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OVV
- Type
- protein
- Length
- 105 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SH3 and multiple ankyrin repeat domains protein 3; Leucine zipper putative tumor…
- UniProt
- A0A0U1RRP5, Q8K1Q4
- Ligands
- ACE, SCN
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SH3 and multiple ankyrin repeat domains protein 3 | protein | 99 | 17% helix, 36% strand | A0A0U1RRP5 |
| B | Leucine zipper putative tumor suppressor 3 | protein | 6 | 0% helix, 67% strand | Q8K1Q4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 522 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5OVV · PDZ domain from rat Shank3 bound to the C terminus of ProSAPiP1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8K1Q4 · AlphaFold monomer V2.0 prediction for leucine zipper putative tumor suppressor 3 (Q8K1Q4) · a predicted model of the same protein · chain B against A, TM-score 0.74
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 A0A0U1RRP5
- Every structure of UniProt Q8K1Q4
- Elsewhere: RCSB PDB 5OVV · PDBe 5OVV · UniProt A0A0U1RRP5 · UniProt Q8K1Q4
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