MolNFT v1 · #119473 · protein
Breaking down the wall: mutation of the tyrosine gate of the universal escherichia COLI fimbrial adhesin fimh
5FX3: “Breaking down the wall: mutation of the tyrosine gate of the universal escherichia COLI fimbrial adhesin fimh”. X-ray diffraction, 1 ligand (EDT). MolNFT v1 #119473 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5FX3
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimh
- UniProt
- Q9S497
- Ligands
- EDT
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fimh | protein | 158 | 6% helix, 53% strand | Q9S497 |
Ligands and binding sites
- EDT · {[-(bis-carboxymethyl-amino)-ethyl]-carboxymethyl-amino}-acetic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, acetylation).
Compared structures
- 5FX3 · Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli… · 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 Q9S497
- Elsewhere: RCSB PDB 5FX3 · PDBe 5FX3 · UniProt Q9S497
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