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Crystal structure of histo-aspartic protease (hap) zymogen from plasmodium falciparum
Analyse Crystal structure of histo-aspartic protease (hap) zymogen from plasmodium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QVC
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histo-aspartic protease
- UniProt
- Q9Y006
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histo-aspartic protease | protein | 368 | 18% helix, 44% strand | Q9Y006 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 765 | 0.76 | 0.80 | 65 | empty |
| 2 | 50 | 0.23 | 0.72 | 15 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3QVC · Crystal structure of histo-aspartic protease (HAP) zymogen from Plasmodium falciparum · 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 Q9Y006
- Elsewhere: RCSB PDB 3QVC · PDBe 3QVC · UniProt Q9Y006
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