Research workbench
Crystal structure of the PAAA2-PARE2 antitoxin-toxin complex
Analyse Crystal structure of the PAAA2-PARE2 antitoxin-toxin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CZF
- Type
- protein
- Length
- 270 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PAAA2; Plasmid stabilization protein pare
- UniProt
- A0A0F6F6Q9, A0A0D7C2L1
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PAAA2 | protein | 45 | 76% helix, 4% strand | A0A0F6F6Q9 |
| B | PAAA2 | protein | 40 | 75% helix, 5% strand | A0A0F6F6Q9 |
| C | Plasmid stabilization protein pare | protein | 93 | 37% helix, 27% strand | A0A0D7C2L1 |
| D | Plasmid stabilization protein pare | protein | 92 | 37% helix, 27% strand | A0A0D7C2L1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.63 | 0.77 | 54 | empty |
| 2 | 51 | 0.26 | 0.73 | 8 | empty |
Interfaces
3 interfaces between chains.
- A–D · 1481 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1445 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 447 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5CZF · Crystal structure of the PaaA2-ParE2 antitoxin-toxin complex · 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 A0A0F6F6Q9
- Every structure of UniProt A0A0D7C2L1
- Elsewhere: RCSB PDB 5CZF · PDBe 5CZF · UniProt A0A0F6F6Q9 · UniProt A0A0D7C2L1
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