Research workbench
Crystal structure of fimh in complex with heptylmannoside
Analyse Crystal structure of fimh in complex with heptylmannoside in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LOV
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein fimh
- UniProt
- P08191
- Ligands
- KGM, NA
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fimh | protein | 158 | 6% helix, 53% strand | P08191 |
Ligands and binding sites
- KGM · heptyl alpha-D-mannopyranoside · ligand · chains A
- NA · Sodium ion · metal · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4LOV · Crystal structure of FimH in complex with Heptylmannoside · the same entry in another collection · chain A against A, TM-score 1.00
- P08191 · AlphaFold monomer V2.0 prediction for type 1 fimbrin D-mannose specific adhesin (P08191) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P08191
- Elsewhere: RCSB PDB 4LOV · PDBe 4LOV · UniProt P08191
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