Research workbench
Fdec, a novel broadly conserved escherichia COLI adhesin eliciting protection against urinary tract infections
Analyse Fdec, a novel broadly conserved escherichia COLI adhesin eliciting protection… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E9L
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Attaching and effacing protein, pathogenesis factor
- UniProt
- Q1RFP2
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Attaching and effacing protein, pathogenesis factor | protein | 314 | 4% helix, 47% strand | Q1RFP2 |
Compared structures
- 4E9L · FdeC, a Novel Broadly Conserved Escherichia coli Adhesin Eliciting Protection against… · 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 Q1RFP2
- Elsewhere: RCSB PDB 4E9L · PDBe 4E9L · UniProt Q1RFP2
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