Research workbench
Synapse associated protein 97 PDZ2 domain variant C378G with C- terminal glur-a peptide
Analyse Synapse associated protein 97 PDZ2 domain variant C378G with C- terminal glur-a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AWW
- Type
- protein
- Length
- 186 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synapse associated protein 97; 18-residue C-terminal peptide from glutamate receptor…
- UniProt
- Q62696
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synapse associated protein 97 | protein | 91 | 15% helix, 37% strand | Q62696 |
| B | Synapse associated protein 97 | protein | 91 | 4% helix, 37% strand | Q62696 |
| C | 18-residue C-terminal peptide from glutamate receptor, ionotropic, AMPA1 | protein | 4 | 0% helix, 50% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.38 | 0.74 | 18 | empty |
Interfaces
2 interfaces between chains.
- A–C · 319 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 39 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2AWW · Synapse associated protein 97 PDZ2 domain variant C378G with C-terminal GluR-A peptide · the same entry in another collection · chain A against A, TM-score 1.00
- Q62696 · AlphaFold monomer V2.0 prediction for disks large homolog 1 (Q62696) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q62696
- Elsewhere: RCSB PDB 2AWW · PDBe 2AWW · UniProt Q62696
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