Research workbench
High resolution structure of the functional region of CWP19 from clostridium difficile
Analyse High resolution structure of the functional region of CWP19 from clostridium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OQ3
- Type
- protein
- Length
- 358 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CWP19
- EC
- 3.5.1.28
- UniProt
- L7PGA3
- Ligands
- CL
- Pockets
- 3 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CWP19 (EC 3.5.1.28) | protein | 358 | 41% helix, 16% strand | L7PGA3 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · 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 | 126 | 0.39 | 0.74 | 26 | empty |
| 2 | 93 | 0.37 | 0.75 | 17 | empty |
| 3 | 64 | 0.30 | 0.74 | 14 | empty |
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 L7PGA3
- Elsewhere: RCSB PDB 5OQ3 · PDBe 5OQ3 · UniProt L7PGA3
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