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Crystal structure of rhogdi E154A,E155A mutant
Analyse Crystal structure of rhogdi E154A,E155A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JHV
- Type
- protein
- Length
- 828 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho GDP-dissociation inhibitor 1
- UniProt
- P52565
- Pockets
- 7 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Rho GDP-dissociation inhibitor 1 | protein | 138 | 7% helix, 56% strand | P52565 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 507 | 0.66 | 0.78 | 60 | empty |
| 2 | 259 | 0.63 | 0.81 | 39 | empty |
| 3 | 262 | 0.63 | 0.81 | 36 | empty |
| 4 | 101 | 0.45 | 0.79 | 19 | empty |
| 5 | 85 | 0.44 | 0.79 | 18 | empty |
Interfaces
5 interfaces between chains.
- C–F · 610 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 595 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 594 Ų buried · 0 hydrogen bonds · protein-protein
- B–F · 335 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 202 Ų buried · 3 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 P52565
- Elsewhere: RCSB PDB 2JHV · PDBe 2JHV · UniProt P52565
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