Research workbench
Mbp-fusion protein of PILA1 from C. difficile R20291 residues 26-166
Analyse Mbp-fusion protein of PILA1 from C. difficile R20291 residues 26-166 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TSM
- Type
- protein
- Length
- 1,529 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding protein, pilin chimera
- UniProt
- D8A942, C9YRY2
- Ligands
- TMO, GLC
- Pockets
- 12 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding protein, pilin chimera | protein | 505 | 42% helix, 22% strand | D8A942, C9YRY2 |
| B, C | Maltose-binding protein, pilin chimera | protein | 512 | 41% helix, 22% strand | D8A942, C9YRY2 |
Ligands and binding sites
- TMO · trimethylamine oxide · ligand · 19 copies · chains A, C, B
- GLC · alpha-D-glucopyranose · sugar · 12 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 948 | 0.79 | 0.81 | 75 | GLC |
| 2 | 1122 | 0.78 | 0.80 | 101 | GLC, TMO |
| 3 | 793 | 0.74 | 0.79 | 74 | TMO |
| 4 | 714 | 0.72 | 0.78 | 90 | TMO |
| 5 | 410 | 0.71 | 0.82 | 33 | GLC |
Interfaces
3 interfaces between chains.
- A–B · 1314 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1057 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 211 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4TSM · MBP-fusion protein of PilA1 from C. difficile R20291 residues 26-166 · 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 D8A942
- Every structure of UniProt C9YRY2
- Elsewhere: RCSB PDB 4TSM · PDBe 4TSM · UniProt D8A942 · UniProt C9YRY2
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