Research workbench
Crystal structure of conserved hypothetical protein SAV0927 from staphylococcus aureus subsp. aureus MU50
Analyse Crystal structure of conserved hypothetical protein SAV0927 from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IY0
- Type
- protein
- Length
- 727 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SAV0927
- UniProt
- A0A0H3JQV2
- Ligands
- CL
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 9 distinct chains · 24% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SAV0927 | protein | 70 | 30% helix, 43% strand | A0A0H3JQV2 |
| B | SAV0927 | protein | 72 | 21% helix, 43% strand | A0A0H3JQV2 |
| C | SAV0927 | protein | 85 | 29% helix, 44% strand | A0A0H3JQV2 |
| D | SAV0927 | protein | 84 | 29% helix, 45% strand | A0A0H3JQV2 |
| E, F | SAV0927 | protein | 88 | 26% helix, 44% strand | A0A0H3JQV2 |
| G | SAV0927 | protein | 86 | 27% helix, 43% strand | A0A0H3JQV2 |
| H | SAV0927 | protein | 87 | 29% helix, 44% strand | A0A0H3JQV2 |
| I | SAV0927 | protein | 35 | 0% helix, 40% strand | A0A0H3JQV2 |
| J | SAV0927 | protein | 32 | 0% helix, 50% strand | A0A0H3JQV2 |
Ligands and binding sites
- CL · Chloride ion · ion · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 606 | 0.70 | 0.78 | 53 | empty |
| 2 | 601 | 0.69 | 0.78 | 57 | empty |
| 3 | 487 | 0.67 | 0.79 | 47 | empty |
| 4 | 221 | 0.57 | 0.79 | 27 | empty |
| 5 | 52 | 0.36 | 0.79 | 12 | empty |
Interfaces
17 interfaces between chains.
- E–F · 2047 Ų buried · 46 hydrogen bonds · protein-protein
- G–H · 1984 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 1892 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 1553 Ų buried · 31 hydrogen bonds · protein-protein
- I–J · 861 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 modified (engineered).
Compared structures
- 6IY0 · Crystal structure of conserved hypothetical protein SAV0927 from Staphylococcus aureus… · 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 A0A0H3JQV2
- Elsewhere: RCSB PDB 6IY0 · PDBe 6IY0 · UniProt A0A0H3JQV2
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