Research workbench
Crystal structure of the catalytic domain of plasmodium falciparum arf GTPase activating protein
Analyse Crystal structure of the catalytic domain of plasmodium falciparum arf GTPase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SUB
- Type
- protein
- Length
- 270 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ADP-ribosylation factor GTPase-activating protein
- UniProt
- Q8I4Y5
- Ligands
- ZN, SO4
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ADP-ribosylation factor GTPase-activating protein | protein | 139 | 50% helix, 9% strand | Q8I4Y5 |
| B | ADP-ribosylation factor GTPase-activating protein | protein | 131 | 50% helix, 10% strand | Q8I4Y5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.81 | 0.92 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3SUB · Crystal structure of the catalytic domain of Plasmodium falciparum ARF GTPase activating… · 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 Q8I4Y5
- Elsewhere: RCSB PDB 3SUB · PDBe 3SUB · UniProt Q8I4Y5
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