Research workbench
Crystal structure of the pleckstrin homology domain of ARHGAP27
Analyse Crystal structure of the pleckstrin homology domain of ARHGAP27 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PP2
- Type
- protein
- Length
- 222 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Rho GTPase-activating protein 27
- UniProt
- Q6ZUM4
- Ligands
- UNX
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rho GTPase-activating protein 27 | protein | 112 | 20% helix, 44% strand | Q6ZUM4 |
| B | Rho GTPase-activating protein 27 | protein | 110 | 16% helix, 43% strand | Q6ZUM4 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 25 copies · chains A, B
- CIT · Citric acid · additive · 5 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 68 | 0.32 | 0.75 | 16 | UNX |
Interfaces
1 interface between chains.
- A–B · 611 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3PP2 · Crystal structure of the pleckstrin homology domain of ArhGAP27 · the same entry in another collection · chain A against A, TM-score 1.00
- Q6ZUM4 · AlphaFold monomer V2.0 prediction for rho GTPase-activating protein 27 (Q6ZUM4) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q6ZUM4
- Elsewhere: RCSB PDB 3PP2 · PDBe 3PP2 · UniProt Q6ZUM4
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