Electrophilic catalysis in triosephosphase isomerase: the role of histidine-95. Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Apr 1993.
Explore 3YPI in 3D Show helices and sheets RCSB PDB PDBe
3YPI contains 27 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 | 3-5 | 3 | |
| β-strand | 6-10 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| α-helix | 17-29 | 13 | |
| β-strand | 37-41 | 5 | 1 |
| α-helix | 44-46 | 3 | |
| α-helix | 47-53 | 7 | |
| β-strand | 59-63 | 5 | 1 |
| β-strand | 72 | 1 | 3 |
| α-helix | 80-86 | 7 | |
| β-strand | 90-93 | 4 | 1 |
| 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 | 178-196 | 19 | |
| α-helix | 198-203 | 6 | |
| β-strand | 205-209 | 5 | 1 |
| α-helix | 214-217 | 4 | |
| α-helix | 218-220 | 3 | |
| β-strand | 228-231 | 4 | 1 |
| α-helix | 233-236 | 4 | |
| α-helix | 240-244 | 5 |
| 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 | 38-41 | 4 | 4 |
| α-helix | 44-46 | 3 | |
| α-helix | 47-53 | 7 | |
| β-strand | 59-63 | 5 | 4 |
| β-strand | 72 | 1 | 2 |
| α-helix | 80-86 | 7 | |
| β-strand | 90-93 | 4 | 4 |
| α-helix | 96-99 | 4 | |
| α-helix | 106-118 | 13 | |
| β-strand | 122-127 | 6 | 4 |
| α-helix | 131-136 | 6 | |
| α-helix | 139-153 | 15 | |
| β-strand | 160-164 | 5 | 4 |
| α-helix | 178-203 | 26 | |
| β-strand | 205-208 | 4 | 4 |
| β-strand | 228-231 | 4 | 4 |
| α-helix | 233-235 | 3 | |
| α-helix | 239-244 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Triosephosphate isomerase | A, B | protein | 247 | Saccharomyces cerevisiae | P00942 (AlphaFold model) |
>3YPI_1 TRIOSEPHOSPHATE ISOMERASE (chains A, B) ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTV GAQNAYLKASGAFTGENSVDQIKDVGAKWVILGQSERRSYFHEDDKFIADKTKFALGQGV GVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDA QDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFV DIINSRN
| ID | Name | Formula | Copies |
|---|---|---|---|
| PGH | Phosphoglycolohydroxamic acid | C2 H6 N O6 P | 2 |
Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95. Komives, E.A., Chang, L.C., Lolis, E. et al. Biochemistry (1991) 30:3011-3019. DOI 10.1021/bi00226a005 · PubMed
Other PDB entries of the same protein (UniProt P00942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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