Research workbench
Crystal structure of C5321: a protective antigen present in uropathogenic escherichia COLI strains displaying an slr fold
Analyse Crystal structure of C5321: a protective antigen present in uropathogenic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BWR
- Type
- protein
- Length
- 467 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein corresponding to locus C5321 from CFT073 E.COLI strain
- UniProt
- Q8FAG2
- Ligands
- MG, CL
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein corresponding to locus C5321 from CFT073 E.COLI strain | protein | 467 | 72% helix, 0% strand | Q8FAG2 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 29 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 4BWR · Crystal structure of c5321: a protective antigen present in uropathogenic Escherichia… · 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 Q8FAG2
- Elsewhere: RCSB PDB 4BWR · PDBe 4BWR · UniProt Q8FAG2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.