Research workbench
Staphylococcus aureus surface protein-sdrc
Analyse Staphylococcus aureus surface protein-sdrc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LXH
- Type
- protein
- Length
- 920 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ser-asp rich fibrinogen-binding, bone sialoprotein-binding protein
- UniProt
- Q2UWJ6
- Pockets
- 11 · best druggability 0.79
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ser-asp rich fibrinogen-binding, bone sialoprotein-binding protein | protein | 308 | 5% helix, 53% strand | Q2UWJ6 |
| B | Ser-asp rich fibrinogen-binding, bone sialoprotein-binding protein | protein | 298 | 6% helix, 51% strand | Q2UWJ6 |
| C | Ser-asp rich fibrinogen-binding, bone sialoprotein-binding protein | protein | 314 | 5% helix, 54% strand | Q2UWJ6 |
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 913 | 0.79 | 0.82 | 109 | empty |
| 2 | 408 | 0.75 | 0.85 | 48 | empty |
| 3 | 259 | 0.60 | 0.80 | 41 | empty |
| 4 | 204 | 0.50 | 0.76 | 30 | empty |
| 5 | 189 | 0.48 | 0.75 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1736 Ų buried · 38 hydrogen bonds · protein-protein
- B–C · 1415 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 26 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6LXH · Staphylococcus aureus surface protein-sdrc · 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 Q2UWJ6
- Elsewhere: RCSB PDB 6LXH · PDBe 6LXH · UniProt Q2UWJ6
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