Phosphofructokinase, inhibited T-state. Determined by X-ray diffraction at 2.6 Å resolution. Released 11 Jul 1996.
Explore 6PFK in 3D Show helices and sheets RCSB PDB PDBe
6PFK contains 60 α-helices and 60 β-strands across 4 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 | 3-9 | 7 | 1 |
| α-helix | 16-29 | 14 | |
| β-strand | 33-37 | 5 | 1 |
| α-helix | 40-46 | 7 | |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 54-57 | 4 | |
| β-strand | 70 | 1 | 2 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-92 | 14 | |
| β-strand | 96-101 | 6 | 1 |
| α-helix | 103-114 | 12 | |
| β-strand | 119-123 | 5 | 1 |
| β-strand | 124 | 1 | 3 |
| β-strand | 137 | 1 | 3 |
| α-helix | 139-155 | 17 | |
| β-strand | 158 | 1 | 4 |
| β-strand | 163-168 | 6 | 5 |
| α-helix | 175-183 | 9 | |
| β-strand | 188-190 | 3 | 5 |
| α-helix | 198-211 | 14 | |
| β-strand | 216-221 | 6 | 5 |
| α-helix | 227-238 | 12 | |
| β-strand | 242-246 | 5 | 5 |
| α-helix | 248-252 | 5 | |
| α-helix | 258-276 | 19 | |
| β-strand | 282-287 | 6 | 1 |
| β-strand | 290-295 | 6 | 1 |
| α-helix | 296-301 | 6 | |
| α-helix | 309-318 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 6 |
| α-helix | 16-29 | 14 | |
| β-strand | 33-37 | 5 | 6 |
| α-helix | 40-45 | 6 | |
| β-strand | 49-51 | 3 | 6 |
| α-helix | 54-57 | 4 | |
| β-strand | 70 | 1 | 7 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-92 | 14 | |
| β-strand | 96-101 | 6 | 6 |
| α-helix | 103-114 | 12 | |
| β-strand | 119-123 | 5 | 6 |
| β-strand | 124-125 | 2 | 8 |
| β-strand | 137-138 | 2 | 8 |
| α-helix | 139-155 | 17 | |
| β-strand | 158 | 1 | 9 |
| β-strand | 163-168 | 6 | 10 |
| α-helix | 175-184 | 10 | |
| β-strand | 188-190 | 3 | 10 |
| α-helix | 198-211 | 14 | |
| β-strand | 216-221 | 6 | 10 |
| α-helix | 222-224 | 3 | |
| α-helix | 227-238 | 12 | |
| β-strand | 242-246 | 5 | 10 |
| α-helix | 248-252 | 5 | |
| α-helix | 258-276 | 19 | |
| β-strand | 282-287 | 6 | 6 |
| β-strand | 290-295 | 6 | 6 |
| α-helix | 296-300 | 5 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-318 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-8 | 6 | 11 |
| α-helix | 16-30 | 15 | |
| β-strand | 33-37 | 5 | 11 |
| α-helix | 40-46 | 7 | |
| β-strand | 49-52 | 4 | 11 |
| α-helix | 54-57 | 4 | |
| β-strand | 70 | 1 | 9 |
| α-helix | 75-77 | 3 | |
| α-helix | 79-92 | 14 | |
| β-strand | 97-101 | 5 | 11 |
| α-helix | 103-114 | 12 | |
| β-strand | 119-123 | 5 | 11 |
| β-strand | 124-125 | 2 | 12 |
| β-strand | 137-138 | 2 | 12 |
| α-helix | 139-155 | 17 | |
| β-strand | 158 | 1 | 7 |
| β-strand | 163-168 | 6 | 10 |
| α-helix | 175-183 | 9 | |
| β-strand | 188-190 | 3 | 10 |
| α-helix | 198-211 | 14 | |
| β-strand | 216-221 | 6 | 10 |
| α-helix | 222-224 | 3 | |
| α-helix | 227-238 | 12 | |
| β-strand | 242-246 | 5 | 10 |
| α-helix | 248-252 | 5 | |
| α-helix | 258-277 | 20 | |
| β-strand | 282-287 | 6 | 11 |
| β-strand | 290-295 | 6 | 11 |
| α-helix | 296-300 | 5 | |
| α-helix | 309-318 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 13 |
| α-helix | 16-29 | 14 | |
| β-strand | 33-37 | 5 | 13 |
| α-helix | 40-46 | 7 | |
| β-strand | 49-52 | 4 | 13 |
| α-helix | 54-57 | 4 | |
| β-strand | 70 | 1 | 4 |
| α-helix | 74-76 | 3 | |
| α-helix | 79-91 | 13 | |
| β-strand | 96-101 | 6 | 13 |
| α-helix | 103-113 | 11 | |
| β-strand | 119-123 | 5 | 13 |
| β-strand | 124-125 | 2 | 14 |
| β-strand | 137-138 | 2 | 14 |
| α-helix | 139-155 | 17 | |
| β-strand | 158 | 1 | 2 |
| β-strand | 163-168 | 6 | 5 |
| α-helix | 175-184 | 10 | |
| β-strand | 188-190 | 3 | 5 |
| α-helix | 198-210 | 13 | |
| β-strand | 216-221 | 6 | 5 |
| α-helix | 227-238 | 12 | |
| β-strand | 242-246 | 5 | 5 |
| α-helix | 248-250 | 3 | |
| α-helix | 258-276 | 19 | |
| β-strand | 282-287 | 6 | 13 |
| β-strand | 290-295 | 6 | 13 |
| α-helix | 296-301 | 6 | |
| α-helix | 304-305 | 2 | |
| α-helix | 309-318 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phosphofructokinase | A, B, C, D | protein | 319 | Geobacillus stearothermophilus | P00512 (AlphaFold model) |
>6PFK_1 PHOSPHOFRUCTOKINASE (chains A, B, C, D) MKRIGVLTSGGDSPGMNAAIRSVVRKAIYHGVEVYGVYHGYAGLIAGNIKKLEVGDVGDI IHRGGTILYTARCPEFKTEEGQKKGIEQLKKHGIEGLVVIGGDGSYQGAKKLTEHGFPCV GVPGTIDNDIPGTDFTIGFDTALNTVIDAIDKIRDTATSHERTYVIEVMGRHAGDIALWS GLAGGAETILIPEADYDMNDVIARLKRGHERGKKHSIIIVAEGVGSGVDFGRQIQEATGF ETRVTVLGHVQRGGSPTAFDRVLASRLGARAVELLLEGKGGRCVGIQNNQLVDHDIAEAL ANKHTIDQRMYALSKELSI
| ID | Name | Formula | Copies |
|---|---|---|---|
| PGA | 2-phosphoglycolic acid | C2 H5 O6 P | 4 |
Structural basis of the allosteric behaviour of phosphofructokinase. Schirmer, T., Evans, P.R. Nature (1990) 343:140-145. DOI 10.1038/343140a0 · PubMed
Other PDB entries of the same protein (UniProt P00512 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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