Research workbench
A thermally stabilised version of plasmodium falciparum RH5
Analyse A thermally stabilised version of plasmodium falciparum RH5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5MI0
- Type
- protein
- Length
- 719 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Reticulocyte binding-like protein 5,RETICULOCYTE binding protein 5; Monoclonal antibody…
- UniProt
- A0A159SJI5, B2L3N7
- Pockets
- 9 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Reticulocyte binding-like protein 5,RETICULOCYTE binding protein 5 | protein | 281 | 81% helix, 4% strand | A0A159SJI5, B2L3N7 |
| B | Monoclonal antibody 9AD4 | protein | 221 | 8% helix, 54% strand | — |
| C | Monoclonal antibody 9AD4 | protein | 217 | 6% helix, 54% strand | — |
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.59 | 0.83 | 22 | empty |
| 2 | 281 | 0.52 | 0.74 | 38 | empty |
| 3 | 112 | 0.50 | 0.81 | 22 | empty |
| 4 | 174 | 0.50 | 0.77 | 23 | empty |
| 5 | 109 | 0.48 | 0.79 | 18 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1936 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 666 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 230 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 5MI0 · A thermally stabilised version of Plasmodium falciparum RH5 · 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 A0A159SJI5
- Every structure of UniProt B2L3N7
- Elsewhere: RCSB PDB 5MI0 · PDBe 5MI0 · UniProt A0A159SJI5 · UniProt B2L3N7
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