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Crystal Structure of the C-terminal half of the Vibrio cholerae minor pilin TcpB
Analyse Crystal Structure of the C-terminal half of the Vibrio cholerae minor pilin TcpB in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MIC
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.531
- Source
- Vibrio cholerae serotype O1
- Molecule
- Toxin co-regulated pilus biosynthesis protein B
- UniProt
- A0A0H3AKH0
Structure
x-ray diffraction · resolution 1.531 · 1 distinct chain · 0% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Toxin co-regulated pilus biosynthesis protein B | protein | 164 | 0% helix, 48% strand | A0A0H3AKH0 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6MIC · Crystal structure of the C-terminal half of the vibrio cholerae minor pilin tcpb · 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 A0A0H3AKH0
- Elsewhere: RCSB PDB 6MIC · PDBe 6MIC · UniProt A0A0H3AKH0
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