Research workbench
Solution structure of the pH domain of human docking protein BRDG1
Analyse Solution structure of the pH domain of human docking protein BRDG1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X1F
- Type
- protein
- Length
- 149 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Signal-transducing adaptor protein 1
- UniProt
- Q9ULZ2
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · 1 distinct chain · 23% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal-transducing adaptor protein 1 | protein | 149 | 23% helix, 26% strand | Q9ULZ2 |
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 | 117 | 0.38 | 0.74 | 18 | empty |
Compared structures
- 1X1F · Solution structure of the PH domain of human Docking protein BRDG1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULZ2 · AlphaFold monomer V2.0 prediction for signal-transducing adaptor protein 1 (Q9ULZ2) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 Q9ULZ2
- Elsewhere: RCSB PDB 1X1F · PDBe 1X1F · UniProt Q9ULZ2
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