Research workbench
Structural and functional attributes of malaria parasite AP4A hydrolase
Analyse Structural and functional attributes of malaria parasite AP4A hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CFJ
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BIS(5'-nucleosyl)-tetraphosphatase (diadenosine tetraphosphatase), putative
- EC
- 3.6.1.17
- UniProt
- C0H4F3
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BIS(5'-nucleosyl)-tetraphosphatase (diadenosine tetraphosphatase), putative (EC 3.6.1.17) | protein | 140 | 24% helix, 41% strand | C0H4F3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5CFJ · Structural and functional attributes of malaria parasite Ap4A hydrolase · 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 C0H4F3
- Elsewhere: RCSB PDB 5CFJ · PDBe 5CFJ · UniProt C0H4F3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.