Research workbench
Structure of C-terminal truncated plasmodium falciparum imp- nucleotidase
Analyse Structure of C-terminal truncated plasmodium falciparum imp- nucleotidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RNH
- Type
- protein
- Length
- 785 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imp-specific 5'-nucleotidase, putative
- EC
- 3.1.3.5
- UniProt
- A0A144A134
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Imp-specific 5'-nucleotidase, putative (EC 3.1.3.5) | protein | 412 | 50% helix, 12% strand | A0A144A134 |
| B | Imp-specific 5'-nucleotidase, putative (EC 3.1.3.5) | protein | 373 | 48% helix, 15% strand | A0A144A134 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1031 | 0.82 | 0.83 | 97 | GOL |
| 2 | 261 | 0.78 | 0.90 | 43 | empty |
| 3 | 292 | 0.59 | 0.78 | 36 | empty |
| 4 | 182 | 0.53 | 0.78 | 22 | empty |
| 5 | 235 | 0.53 | 0.76 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 962 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6RNH · Structure of C-terminal truncated Plasmodium falciparum IMP-nucleotidase · 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 A0A144A134
- Elsewhere: RCSB PDB 6RNH · PDBe 6RNH · UniProt A0A144A134
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