Research workbench
Crystal structure of the phosphotyrosin binding DOMAIN(PTB) of mouse disabled 1(DAB1)
Analyse Crystal structure of the phosphotyrosin binding DOMAIN(PTB) of mouse disabled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1P3R
- Type
- protein
- Length
- 442 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disabled homolog 2
- UniProt
- P98078
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disabled homolog 2 | protein | 148 | 35% helix, 35% strand | P98078 |
| B | Disabled homolog 2 | protein | 148 | 35% helix, 35% strand | P98078 |
| C | Disabled homolog 2 | protein | 146 | 35% helix, 36% strand | P98078 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1142 | 0.78 | 0.80 | 85 | empty |
| 2 | 151 | 0.48 | 0.78 | 29 | empty |
| 3 | 175 | 0.43 | 0.74 | 32 | empty |
Interfaces
3 interfaces between chains.
- B–C · 557 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 415 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 270 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1P3R · Crystal structure of the phosphotyrosin binding domain(PTB) of mouse Disabled 1(Dab1) · the same entry in another collection · chain A against A, TM-score 1.00
- P98078 · AlphaFold monomer V2.0 prediction for disabled homolog 2 (P98078) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P98078
- Elsewhere: RCSB PDB 1P3R · PDBe 1P3R · UniProt P98078
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