MolNFT v1 · #29811 · protein
Escherichia COLI F17FG lectin domain complex with N-acetylglucosamine
1ZK5 · F17G adhesin subunit: “Escherichia COLI F17FG lectin domain complex with N-acetylglucosamine”. X-ray diffraction, 1 ligand (NAG). MolNFT v1 #29811 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1ZK5
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F17G adhesin subunit
- UniProt
- Q9RH91
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F17G adhesin subunit | protein | 172 | 2% helix, 58% strand | Q9RH91 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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
- 1ZK5 · Escherichia coli F17fG lectin domain complex with N-acetylglucosamine · the same entry in another collection · chain A against A, TM-score 1.00
- Q9RH91 · AlphaFold monomer V2.0 prediction for F17F-G fimbrial adhesin (Q9RH91) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q9RH91
- Elsewhere: RCSB PDB 1ZK5 · PDBe 1ZK5 · UniProt Q9RH91
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