Crystal structure of human 5T4 (Wnt-activated inhibitory factor 1, Trophoblast glycoprotein). Determined by X-ray diffraction at 1.77 Å resolution. Released 26 Feb 2014.
Explore 4CNC in 3D Show helices and sheets RCSB PDB PDBe
4CNC contains 23 α-helices and 36 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 67-69 | 3 | 1 |
| β-strand | 74-76 | 3 | 1 |
| β-strand | 95-97 | 3 | 1 |
| β-strand | 104-106 | 3 | 2 |
| β-strand | 122-124 | 3 | 1 |
| β-strand | 130-133 | 4 | 2 |
| β-strand | 146-148 | 3 | 1 |
| β-strand | 156-157 | 2 | 2 |
| β-strand | 177-179 | 3 | 1 |
| α-helix | 184-186 | 3 | |
| α-helix | 195-204 | 10 | |
| α-helix | 205-207 | 3 | |
| β-strand | 214-216 | 3 | 1 |
| α-helix | 227-232 | 6 | |
| β-strand | 238-240 | 3 | 1 |
| β-strand | 262-264 | 3 | 1 |
| α-helix | 275-282 | 8 | |
| β-strand | 288-290 | 3 | 1 |
| β-strand | 296-297 | 2 | 3 |
| α-helix | 300-302 | 3 | |
| α-helix | 303-311 | 9 | |
| β-strand | 315-316 | 2 | 1 |
| α-helix | 318-320 | 3 | |
| β-strand | 322 | 1 | 4 |
| β-strand | 323-325 | 3 | 3 |
| α-helix | 327-329 | 3 | |
| β-strand | 333 | 1 | 4 |
| α-helix | 334-336 | 3 | |
| α-helix | 339-341 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 61-63 | 3 | |
| β-strand | 67-69 | 3 | 5 |
| β-strand | 74-76 | 3 | 5 |
| β-strand | 95-97 | 3 | 5 |
| β-strand | 104-106 | 3 | 6 |
| β-strand | 122-124 | 3 | 5 |
| β-strand | 130-133 | 4 | 6 |
| β-strand | 146-148 | 3 | 5 |
| β-strand | 156-157 | 2 | 6 |
| β-strand | 177-179 | 3 | 5 |
| α-helix | 195-204 | 10 | |
| α-helix | 205-207 | 3 | |
| β-strand | 214-216 | 3 | 5 |
| α-helix | 227-232 | 6 | |
| β-strand | 238-240 | 3 | 5 |
| α-helix | 254-256 | 3 | |
| β-strand | 262-264 | 3 | 5 |
| α-helix | 275-281 | 7 | |
| β-strand | 288-290 | 3 | 5 |
| β-strand | 296-297 | 2 | 7 |
| α-helix | 300-302 | 3 | |
| α-helix | 303-311 | 9 | |
| β-strand | 315-316 | 2 | 5 |
| α-helix | 318-320 | 3 | |
| β-strand | 322 | 1 | 8 |
| β-strand | 323-325 | 3 | 7 |
| α-helix | 327-329 | 3 | |
| β-strand | 333 | 1 | 8 |
| α-helix | 334-336 | 3 | |
| α-helix | 339-341 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trophoblast glycoprotein | A, B | protein | 299 | HOMO SAPIENS | Q13641 (AlphaFold model) |
>4CNC_1 TROPHOBLAST GLYCOPROTEIN (chains A, B) ETGDQCPALCECSEAARTVKCVNRNLTEVPTDLPAYVRNLFLTGNQLAVLPAGAFARRPP LAELAALNLSGSRLDEVRAGAFEHLPSLRQLDLSHNPLADLSPFAFSGSNASVSAPSPLV ELILNHIVPPEDERQNRSFEGMVVAALLAGRALQGLRRLELASNHFLYLPRDVLAQLPSL RHLDLSNNSLVSLTYVSFRNLTHLESLHLEDNALKVLHNGTLAELQGLPHIRVFLDNNPW VCDCHMADMVTWLKETEVVQGKDRLTCAYPEKMRNRVLLELNSADLDCDGTETSQVAPA
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Water and common crystallization additives (NA, SO4, GOL, PEG) are not listed.
Structural Insights Into the Inhibition of Wnt Signaling by Cancer Antigen 5T4/Wnt-Activated Inhibitory Factor 1. Zhao, Y., Malinauskas, T., Harlos, K. et al. Structure (2014) 22:612. DOI 10.1016/J.STR.2014.01.009 · PubMed
Other PDB entries of the same protein (UniProt Q13641 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4CNC directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.