Research workbench
Structure of P. falciparum PFPK5-indirubin-5-sulphonate ligand complex
Analyse Structure of P. falciparum PFPK5-indirubin-5-sulphonate ligand complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V0O
- Type
- protein
- Length
- 550 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell division control protein 2 homolog
- EC
- 2.7.1.-
- UniProt
- Q07785
- Ligands
- INR
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell division control protein 2 homolog (EC 2.7.1.-) | protein | 276 | 35% helix, 18% strand | Q07785 |
| B | Cell division control protein 2 homolog (EC 2.7.1.-) | protein | 274 | 36% helix, 18% strand | Q07785 |
Ligands and binding sites
- INR · 2',3-dioxo-1,1',2',3-tetrahydro-2,3'-biindole-5'-sulfonic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.76 | 0.88 | 43 | INR |
| 2 | 183 | 0.75 | 0.91 | 26 | INR |
| 3 | 222 | 0.57 | 0.79 | 31 | empty |
| 4 | 171 | 0.53 | 0.79 | 37 | empty |
| 5 | 154 | 0.42 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 285 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1V0O · Structure of P. falciparum PfPK5-Indirubin-5-sulphonate ligand complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q07785 · AlphaFold monomer V2.0 prediction for cell division control protein 2 homolog (Q07785) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q07785
- Elsewhere: RCSB PDB 1V0O · PDBe 1V0O · UniProt Q07785
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