Research workbench
Structure of pseudoprotease cspc from clostridioides difficile
Analyse Structure of pseudoprotease cspc from clostridioides difficile in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MW4
- Type
- protein
- Length
- 551 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative germination-specific protease
- UniProt
- C9YNI7
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative germination-specific protease | protein | 551 | 24% helix, 31% strand | C9YNI7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 633 | 0.78 | 0.84 | 94 | SO4 |
| 2 | 133 | 0.48 | 0.79 | 32 | empty |
| 3 | 144 | 0.43 | 0.75 | 23 | empty |
Compared structures
- 6MW4 · Structure of pseudoprotease CspC from Clostridioides difficile · 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 C9YNI7
- Elsewhere: RCSB PDB 6MW4 · PDBe 6MW4 · UniProt C9YNI7
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