Research workbench
Se-sad structure of the functional region of CWP19 from clostridium difficile
Analyse Se-sad structure of the functional region of CWP19 from clostridium difficile in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OQ2
- Type
- protein
- Length
- 719 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CWP19
- EC
- 3.5.1.28
- UniProt
- L7PGA3
- Ligands
- PO4
- Pockets
- 4 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CWP19 (EC 3.5.1.28) | protein | 360 | 39% helix, 16% strand | L7PGA3 |
| B | CWP19 (EC 3.5.1.28) | protein | 359 | 38% helix, 16% strand | L7PGA3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 538 | 0.65 | 0.77 | 61 | empty |
| 2 | 241 | 0.53 | 0.76 | 37 | empty |
| 3 | 138 | 0.42 | 0.75 | 27 | empty |
| 4 | 52 | 0.25 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 254 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 5OQ2 · Se-SAD structure of the functional region of Cwp19 from Clostridium 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 L7PGA3
- Elsewhere: RCSB PDB 5OQ2 · PDBe 5OQ2 · UniProt L7PGA3
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