Research workbench

F17B-G lectin domain with bound GLCNAC(BETA1-2)MAN

Analyse F17B-G lectin domain with bound GLCNAC(BETA1-2)MAN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3FFO
Type: protein
Length: 176 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adhesin
UniProt: Q47200
Ligands: BMA, NAG, NI, SO4

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adhesin	protein	176	2% helix, 57% strand	Q47200

Ligands and binding sites

BMA · beta-D-mannopyranose · sugar · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
NI · Nickel (II) ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · 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

3FFO · F17b-G lectin domain with bound GlcNAc(beta1-2)man · the same entry in another collection · chain A against A, TM-score 1.00
Q47200 · AlphaFold monomer V2.0 prediction for F17B-G fimbrial adhesin (Q47200) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q47200
Elsewhere: RCSB PDB 3FFO · PDBe 3FFO · UniProt Q47200

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.