Research workbench
Structure of the streptococcal endopeptidase ides, a novel cysteine proteinase with strict specificity for IgG
Analyse Structure of the streptococcal endopeptidase ides, a novel cysteine proteinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y08
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein SPY0861
- UniProt
- Q9F1R7
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein SPY0861 | protein | 286 | 25% helix, 24% strand | Q9F1R7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 82 | 0.42 | 0.79 | 16 | SO4 |
| 2 | 86 | 0.31 | 0.73 | 19 | empty |
| 3 | 61 | 0.30 | 0.74 | 12 | empty |
Compared structures
- 1Y08 · Structure of the Streptococcal Endopeptidase IdeS, a Novel Cysteine Proteinase with… · 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 Q9F1R7
- Elsewhere: RCSB PDB 1Y08 · PDBe 1Y08 · UniProt Q9F1R7
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