Research workbench
Crystal structure of the cofa type IV pilin subunit from enterotoxigenic E. COLI
Analyse Crystal structure of the cofa type IV pilin subunit from enterotoxigenic E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S0T
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CFA/III pilin
- UniProt
- Q59393
- Ligands
- NA
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CFA/III pilin | protein | 180 | 30% helix, 19% strand | Q59393 |
| B | CFA/III pilin | protein | 181 | 29% helix, 19% strand | Q59393 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 398 | 0.64 | 0.78 | 40 | empty |
| 2 | 55 | 0.23 | 0.72 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 334 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3S0T · Crystal structure of the CofA Type IV pilin subunit from enterotoxigenic E. coli · 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 Q59393
- Elsewhere: RCSB PDB 3S0T · PDBe 3S0T · UniProt Q59393
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