MolNFT v1 · #125912 · protein
Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from yersinia enterocolitica, in complex with galactose
5LN8 · Fimbrial protein MYFA,FIMBRIAL protein myfa: “Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from yersinia enterocolitica…”. X-ray diffraction, 1 ligand (GAL), 1 pocket (best druggability 0.37).…
- PDB
- 5LN8
- Type
- protein
- Length
- 247 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimbrial protein MYFA,FIMBRIAL protein myfa
- UniProt
- P33406
- Ligands
- GAL
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fimbrial protein MYFA,FIMBRIAL protein myfa | protein | 123 | 2% helix, 56% strand | P33406 |
| B | Fimbrial protein MYFA,FIMBRIAL protein myfa | protein | 124 | 2% helix, 61% strand | P33406 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.37 | 0.79 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5LN8 · Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from… · the same entry in another collection · chain A against A, TM-score 1.00
- P33406 · AlphaFold monomer V2.0 prediction for fimbrial protein myfa (P33406) · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P33406
- Elsewhere: RCSB PDB 5LN8 · PDBe 5LN8 · UniProt P33406
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