Research workbench
Crystal structure of the lectin domain of F18 fimbrial adhesin fedf.
Analyse Crystal structure of the lectin domain of F18 fimbrial adhesin fedf. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B4P
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F18 fimbrial adhesin ac
- UniProt
- Q47212
- Ligands
- BR, SO4
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 65% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F18 fimbrial adhesin ac | protein | 141 | 6% helix, 65% strand | Q47212 |
| B | F18 fimbrial adhesin ac | protein | 142 | 6% helix, 65% strand | Q47212 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 722 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 4B4P · Crystal Structure of the lectin domain of F18 fimbrial adhesin FedF. · 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 Q47212
- Elsewhere: RCSB PDB 4B4P · PDBe 4B4P · UniProt Q47212
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.