Research workbench
PFAMA1 in complex with invasion-inhibitory peptide R1
Analyse PFAMA1 in complex with invasion-inhibitory peptide R1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SRJ
- Type
- protein
- Length
- 647 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Apical membrane antigen 1, AMA1; R1 peptide
- UniProt
- Q7KQK5
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 6 distinct chains · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Apical membrane antigen 1, AMA1 | protein | 298 | 16% helix, 31% strand | Q7KQK5 |
| B | Apical membrane antigen 1, AMA1 | protein | 297 | 16% helix, 31% strand | Q7KQK5 |
| C | R1 peptide | protein | 18 | 0% helix, 22% strand | — |
| D | R1 peptide | protein | 7 | 0% helix, 57% strand | — |
| E | R1 peptide | protein | 17 | 0% helix, 24% strand | — |
| F | R1 peptide | protein | 10 | 0% helix, 40% strand | — |
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.64 | 0.75 | 49 | empty |
| 2 | 115 | 0.57 | 0.84 | 26 | empty |
| 3 | 117 | 0.51 | 0.81 | 25 | empty |
Interfaces
7 interfaces between chains.
- A–C · 1197 Ų buried · 17 hydrogen bonds · protein-protein
- B–E · 1149 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 411 Ų buried · 3 hydrogen bonds · protein-protein
- B–F · 350 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 300 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 3SRJ · PfAMA1 in complex with invasion-inhibitory peptide R1 · 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 Q7KQK5
- Elsewhere: RCSB PDB 3SRJ · PDBe 3SRJ · UniProt Q7KQK5
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