Research workbench
Crystal structure of the second PDZ domain of SAP97 in complex with a glur-a C-terminal peptide
Analyse Crystal structure of the second PDZ domain of SAP97 in complex with a glur-a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G2L
- Type
- protein
- Length
- 185 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synapse-associated protein 97; 18-mer peptide from glutamate receptor, ionotropic, AMPA1
- UniProt
- Q62696
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 3 distinct chains · 15% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Synapse-associated protein 97 | protein | 90 | 16% helix, 40% strand | Q62696 |
| C | 18-mer peptide from glutamate receptor, ionotropic, AMPA1 | protein | 4 | 0% helix, 50% strand | — |
| D | 18-mer peptide from glutamate receptor, ionotropic, AMPA1 | protein | 1 | 0% helix, 0% 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 | 86 | 0.32 | 0.74 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–C · 307 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 182 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 38 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2G2L · Crystal Structure of the Second PDZ Domain of SAP97 in Complex with a GluR-A C-terminal… · 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 2G2L · PDBe 2G2L · UniProt Q62696
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