Research workbench
Crystal structure of rhogef protein asef
Analyse Crystal structure of rhogef protein asef in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DX1
- Type
- protein
- Length
- 385 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho guanine nucleotide exchange factor 4
- UniProt
- Q9NR80
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho guanine nucleotide exchange factor 4 | protein | 385 | 52% helix, 19% strand | Q9NR80 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 515 | 0.71 | 0.81 | 38 | empty |
| 2 | 520 | 0.64 | 0.76 | 50 | empty |
| 3 | 97 | 0.40 | 0.77 | 18 | empty |
| 4 | 93 | 0.39 | 0.76 | 21 | empty |
Modifications
Observed in the structure: 8 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 Q9NR80
- Elsewhere: RCSB PDB 2DX1 · PDBe 2DX1 · UniProt Q9NR80
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