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Crystal structure of human rho GTPase activating protein 15 (ARHGAP15)
Analyse Crystal structure of human rho GTPase activating protein 15 (ARHGAP15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BYI
- Type
- protein
- Length
- 841 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho GTPase activating protein 15
- UniProt
- Q8IXX1
- Pockets
- 9 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Rho GTPase activating protein 15 | protein | 211 | 66% helix, 0% strand | Q8IXX1 |
| C | Rho GTPase activating protein 15 | protein | 210 | 67% helix, 0% strand | Q8IXX1 |
| D | Rho GTPase activating protein 15 | protein | 209 | 65% helix, 0% strand | Q8IXX1 |
Pockets
9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 868 | 0.85 | 0.87 | 78 | empty |
| 2 | 646 | 0.82 | 0.86 | 56 | empty |
| 3 | 607 | 0.80 | 0.85 | 73 | empty |
| 4 | 210 | 0.70 | 0.87 | 28 | empty |
| 5 | 170 | 0.68 | 0.88 | 31 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1248 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 1241 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 580 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 532 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 368 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3BYI · Crystal structure of human Rho GTPase activating protein 15 (ARHGAP15) · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8IXX1
- Elsewhere: RCSB PDB 3BYI · PDBe 3BYI · UniProt Q8IXX1
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