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Crystal structure of the phosphotyrosine binding DOMAIN(PTB) of mouse disabled 2(DAB2):IMPLICATIONS for reeling signaling
Analyse Crystal structure of the phosphotyrosine 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
- 1M7E
- Type
- protein
- Length
- 477 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disabled homolog 2; Ngyenptyk peptide
- UniProt
- P98078
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Disabled homolog 2 | protein | 150 | 37% helix, 35% strand | P98078 |
| D, E, F | Ngyenptyk peptide | protein | 9 | 0% helix, 22% strand | — |
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 | 1108 | 0.79 | 0.80 | 86 | empty |
| 2 | 150 | 0.42 | 0.74 | 25 | empty |
| 3 | 54 | 0.30 | 0.76 | 15 | empty |
Interfaces
7 interfaces between chains.
- A–D · 749 Ų buried · 15 hydrogen bonds · protein-protein
- B–E · 740 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 738 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 521 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 398 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1M7E · Crystal structure of the phosphotyrosine binding domain(PTB) of mouse Disabled… · the same entry in another collection · chain F against F, 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 1M7E · PDBe 1M7E · UniProt P98078
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