Research workbench
Crystal structure of the dh-pH-pH domain of FARP1
Analyse Crystal structure of the dh-pH-pH domain of FARP1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H6Y
- Type
- protein
- Length
- 810 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferm, rhogef and pleckstrin domain-containing protein 1
- UniProt
- Q9Y4F1
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferm, rhogef and pleckstrin domain-containing protein 1 | protein | 402 | 47% helix, 22% strand | Q9Y4F1 |
| B | Ferm, rhogef and pleckstrin domain-containing protein 1 | protein | 408 | 46% helix, 21% strand | Q9Y4F1 |
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 463 | 0.83 | 0.89 | 47 | empty |
| 2 | 558 | 0.76 | 0.83 | 62 | empty |
| 3 | 882 | 0.76 | 0.79 | 99 | empty |
| 4 | 106 | 0.71 | 0.92 | 26 | empty |
| 5 | 51 | 0.67 | 0.97 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 358 Ų buried · 2 hydrogen bonds · protein-protein
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 Q9Y4F1
- Elsewhere: RCSB PDB 4H6Y · PDBe 4H6Y · UniProt Q9Y4F1
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