Structure of C126S mutant of Saccharomyces cerevisiae triosephosphate isomerase. Determined by X-ray diffraction at 1.86 Å resolution. Released 22 Aug 2012.
Explore 4FF7 in 3D Show helices and sheets RCSB PDB PDBe
4FF7 contains 31 α-helices and 20 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 |
|---|---|---|---|
| α-helix | 3-4 | 2 | |
| β-strand | 5-10 | 6 | 1 |
| β-strand | 13 | 1 | 2 |
| α-helix | 17-29 | 13 | |
| β-strand | 36-41 | 6 | 1 |
| α-helix | 44-46 | 3 | |
| α-helix | 47-53 | 7 | |
| β-strand | 59-63 | 5 | 1 |
| β-strand | 72 | 1 | 3 |
| α-helix | 80-85 | 6 | |
| β-strand | 90-93 | 4 | 1 |
| α-helix | 96-101 | 6 | |
| α-helix | 106-118 | 13 | |
| β-strand | 122-127 | 6 | 1 |
| α-helix | 131-135 | 5 | |
| α-helix | 139-153 | 15 | |
| β-strand | 160-164 | 5 | 1 |
| α-helix | 167-169 | 3 | |
| α-helix | 175-177 | 3 | |
| α-helix | 178-196 | 19 | |
| α-helix | 198-203 | 6 | |
| β-strand | 206-209 | 4 | 1 |
| α-helix | 217-220 | 4 | |
| β-strand | 228-231 | 4 | 1 |
| α-helix | 233-236 | 4 | |
| α-helix | 239-244 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 6-10 | 5 | 4 |
| β-strand | 13 | 1 | 3 |
| α-helix | 17-29 | 13 | |
| β-strand | 37-41 | 5 | 4 |
| α-helix | 44-46 | 3 | |
| α-helix | 47-53 | 7 | |
| β-strand | 59-63 | 5 | 4 |
| β-strand | 72 | 1 | 2 |
| α-helix | 80-85 | 6 | |
| β-strand | 90-93 | 4 | 4 |
| α-helix | 96-101 | 6 | |
| α-helix | 106-118 | 13 | |
| β-strand | 122-127 | 6 | 4 |
| α-helix | 131-135 | 5 | |
| α-helix | 139-151 | 13 | |
| β-strand | 160-164 | 5 | 4 |
| α-helix | 167-169 | 3 | |
| α-helix | 178-196 | 19 | |
| α-helix | 198-203 | 6 | |
| β-strand | 206-208 | 3 | 4 |
| α-helix | 217-220 | 4 | |
| β-strand | 228-231 | 4 | 4 |
| α-helix | 233-236 | 4 | |
| α-helix | 240-244 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Triosephosphate isomerase | A, B | protein | 248 | Saccharomyces cerevisiae | P00942 (AlphaFold model) |
>4FF7_1 Triosephosphate isomerase (chains A, B) MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVT VGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQG VGVILSIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPED AQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEF VDIINSRN
Water and common crystallization additives (SO4, NA, GOL) are not listed.
Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Hernandez-Santoyo, A., Dominguez-Ramirez, L., Reyes-Lopez, C.A. et al. Int J Mol Sci (2012) 13:10010-10021. DOI 10.3390/ijms130810010 · PubMed
Other PDB entries of the same protein (UniProt P00942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4FF7 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.