MolNFT v1 · #118459 · protein
Crystal structure of para-biphenyl-2-methyl-3', 5' di-methyl amide mannoside bound to fimh lectin domain
5F2F · Protein fimh: “Crystal structure of para-biphenyl-2-methyl-3', 5' di-methyl amide mannoside bound to fimh lectin domain”. X-ray diffraction, 1 ligand (5U7). MolNFT v1 #118459 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5F2F
- 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
- 5U7
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
- 5U7 · 5-[4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-3-methyl-phenyl]-~{N}1,~{N}3-dimethyl-benzene-1,3-dicarboxamide · ligand · chains A
- GOL · Glycerol · additive · 2 copies · 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
- 5F2F · Crystal structure of para-biphenyl-2-methyl-3', 5' di-methyl amide mannoside bound to… · 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 0.83
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 5F2F · PDBe 5F2F · UniProt P08191
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.