Research workbench
Crystal structure of shaft pilin spaa from lactobacillus rhamnosus gg
Analyse Crystal structure of shaft pilin spaa from lactobacillus rhamnosus gg in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F44
- Type
- protein
- Length
- 785 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cell surface protein spaa
- UniProt
- C7T9P4
- Pockets
- 8 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cell surface protein spaa | protein | 265 | 6% helix, 43% strand | C7T9P4 |
| B | Cell surface protein spaa | protein | 264 | 6% helix, 44% strand | C7T9P4 |
| C | Cell surface protein spaa | protein | 256 | 7% helix, 46% strand | C7T9P4 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.55 | 0.77 | 33 | empty |
| 2 | 104 | 0.47 | 0.80 | 28 | empty |
| 3 | 126 | 0.40 | 0.74 | 27 | empty |
| 4 | 95 | 0.40 | 0.77 | 21 | empty |
| 5 | 89 | 0.36 | 0.75 | 20 | ACT |
Interfaces
1 interface between chains.
- A–B · 804 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 isopeptide (isopeptide).
Compared structures
- 5F44 · Crystal structure of shaft pilin spaA from Lactobacillus rhamnosus GG · 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 C7T9P4
- Elsewhere: RCSB PDB 5F44 · PDBe 5F44 · UniProt C7T9P4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.