Research workbench
Crystal structure of the novel protein and virulence factor ship (Q99XU0) from streptococcus pyogenes
Analyse Crystal structure of the novel protein and virulence factor ship (Q99XU0) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MER
- Type
- protein
- Length
- 376 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Streptococcal histidine-rich glycoprotein interacting protein
- UniProt
- Q99XU0
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 4 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Streptococcal histidine-rich glycoprotein interacting protein | protein | 96 | 80% helix, 0% strand | Q99XU0 |
| B | Streptococcal histidine-rich glycoprotein interacting protein | protein | 95 | 78% helix, 0% strand | Q99XU0 |
| C | Streptococcal histidine-rich glycoprotein interacting protein | protein | 88 | 80% helix, 0% strand | Q99XU0 |
| D | Streptococcal histidine-rich glycoprotein interacting protein | protein | 97 | 78% helix, 0% strand | Q99XU0 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.38 | 0.77 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2821 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 2769 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 422 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 401 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 142 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4MER · Crystal structure of the novel protein and virulence factor sHIP (Q99XU0) from… · 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 Q99XU0
- Elsewhere: RCSB PDB 4MER · PDBe 4MER · UniProt Q99XU0
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