Research workbench
Crystal structure of the dimeric SH2 domain of aps
Analyse Crystal structure of the dimeric SH2 domain of aps in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RPY
- Type
- protein
- Length
- 168 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adaptor protein aps
- UniProt
- Q9Z200
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adaptor protein aps | protein | 82 | 41% helix, 23% strand | Q9Z200 |
| B | Adaptor protein aps | protein | 86 | 36% helix, 23% strand | Q9Z200 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 235 | 0.57 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1235 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (engineered).
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 Q9Z200
- Elsewhere: RCSB PDB 1RPY · PDBe 1RPY · UniProt Q9Z200
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