Research workbench
FAB234 in complex with the C-terminal alpha-tsr domain of P. falciparum
Analyse FAB234 in complex with the C-terminal alpha-tsr domain of P. falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RXI
- Type
- protein
- Length
- 490 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAB234 light chain; FAB234 heavy chain; Circumsporozoite protein
- UniProt
- Q7K740
- Pockets
- 5 · best druggability 0.44
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | FAB234 light chain | protein | 210 | 8% helix, 49% strand | — |
| H | FAB234 heavy chain | protein | 216 | 4% helix, 55% strand | — |
| A | Circumsporozoite protein | protein | 64 | 31% helix, 22% strand | Q7K740 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.44 | 0.81 | 13 | empty |
| 2 | 53 | 0.36 | 0.79 | 12 | empty |
| 3 | 79 | 0.30 | 0.72 | 19 | empty |
| 4 | 69 | 0.29 | 0.73 | 15 | empty |
| 5 | 61 | 0.27 | 0.73 | 20 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1630 Ų buried · 12 hydrogen bonds · protein-protein
- H–A · 651 Ų buried · 12 hydrogen bonds · protein-protein
- L–A · 244 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7RXI · Fab234 in complex with the C-terminal alpha-TSR domain of P. falciparum · the same entry in another collection · chain L against L, 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 Q7K740
- Elsewhere: RCSB PDB 7RXI · PDBe 7RXI · UniProt Q7K740
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.