Research workbench
Structure of a dimeric plasmodium falciparum profilin mutant
Analyse Structure of a dimeric plasmodium falciparum profilin mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D60
- Type
- protein
- Length
- 2,575 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Profilin
- UniProt
- P86294
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, L, M, N, O, P | Profilin | protein | 161 | 22% helix, 41% strand | P86294 |
| K | Profilin | protein | 160 | 26% helix, 41% strand | P86294 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 8 copies · chains A, D, B, C, K, L, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 920 | 0.82 | 0.84 | 88 | SO4 |
| 2 | 964 | 0.79 | 0.81 | 79 | empty |
| 3 | 599 | 0.69 | 0.78 | 55 | empty |
| 4 | 282 | 0.61 | 0.79 | 29 | empty |
| 5 | 300 | 0.61 | 0.79 | 35 | empty |
Interfaces
35 interfaces between chains.
- C–D · 3201 Ų buried · 67 hydrogen bonds · protein-protein
- J–L · 3161 Ų buried · 69 hydrogen bonds · protein-protein
- E–K · 3157 Ų buried · 69 hydrogen bonds · protein-protein
- F–H · 3154 Ų buried · 56 hydrogen bonds · protein-protein
- A–I · 3137 Ų buried · 75 hydrogen bonds · protein-protein
Compared structures
- 4D60 · Structure of a dimeric Plasmodium falciparum profilin mutant · the same entry in another collection · chain P against P, 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 P86294
- Elsewhere: RCSB PDB 4D60 · PDBe 4D60 · UniProt P86294
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