Research workbench
Pilm-piln type IV pilus biogenesis complex
Analyse Pilm-piln type IV pilus biogenesis complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YCH
- Type
- protein
- Length
- 344 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Competence protein pilm; Competence protein piln
- UniProt
- Q5SIJ0, Q5SII9
- Ligands
- ATP, MG
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Competence protein pilm | protein | 336 | 43% helix, 29% strand | Q5SIJ0 |
| B | Competence protein piln | protein | 8 | 0% helix, 0% strand | Q5SII9 |
Ligands and binding sites
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 | 450 | 0.69 | 0.80 | 60 | MG, ATP |
| 2 | 61 | 0.32 | 0.76 | 18 | empty |
| 3 | 50 | 0.26 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 806 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
- 2YCH · PilM-PilN type IV pilus biogenesis complex · 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 Q5SIJ0
- Every structure of UniProt Q5SII9
- Elsewhere: RCSB PDB 2YCH · PDBe 2YCH · UniProt Q5SIJ0 · UniProt Q5SII9
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