Research workbench
Non-canonical staphylococcus aureus pathogenicity island repression.
Analyse Non-canonical staphylococcus aureus pathogenicity island repression. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P4A
- Type
- protein
- Length
- 521 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stl; Sri
- UniProt
- O54475, A0A659I9D5
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 53% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stl | protein | 246 | 57% helix, 6% strand | O54475 |
| E | Sri | protein | 49 | 63% helix, 0% strand | A0A659I9D5 |
| B | Stl | protein | 207 | 50% helix, 5% strand | O54475 |
| D | Sri | protein | 19 | 0% helix, 0% strand | A0A659I9D5 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 901 | 0.80 | 0.82 | 86 | empty |
| 2 | 724 | 0.78 | 0.83 | 73 | empty |
| 3 | 609 | 0.75 | 0.81 | 56 | empty |
| 4 | 98 | 0.40 | 0.77 | 23 | empty |
| 5 | 67 | 0.36 | 0.77 | 17 | empty |
Interfaces
5 interfaces between chains.
- A–B · 4615 Ų buried · 51 hydrogen bonds · protein-protein
- A–E · 724 Ų buried · 4 hydrogen bonds · protein-protein
- E–B · 354 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 281 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 38 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 7P4A · Non-canonical Staphylococcus aureus pathogenicity island repression. · 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 O54475
- Every structure of UniProt A0A659I9D5
- Elsewhere: RCSB PDB 7P4A · PDBe 7P4A · UniProt O54475 · UniProt A0A659I9D5
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