Fructose-1,6-bisphosphate aldolase from rabbit muscle in complex with the inhibitor naphthalene 2,6-bisphosphate. Determined by X-ray diffraction at 1.97 Å resolution. Released 25 Oct 2017.
Explore 5TLZ in 3D Show helices and sheets RCSB PDB PDBe
5TLZ contains 73 α-helices and 54 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 |
|---|---|---|---|
| α-helix | 9-22 | 14 | |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 36-44 | 9 | |
| α-helix | 52-63 | 12 | |
| α-helix | 67-69 | 3 | |
| β-strand | 73-78 | 6 | 1 |
| α-helix | 80-83 | 4 | |
| β-strand | 86 | 1 | 2 |
| β-strand | 92 | 1 | 2 |
| α-helix | 93-99 | 7 | |
| α-helix | 102 | 1 | |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 112-114 | 3 | 3 |
| β-strand | 122-124 | 3 | 3 |
| α-helix | 130-139 | 10 | |
| β-strand | 144-151 | 8 | 1 |
| β-strand | 154 | 1 | 4 |
| β-strand | 157 | 1 | 4 |
| α-helix | 160-179 | 20 | |
| β-strand | 183-190 | 8 | 1 |
| α-helix | 191 | 1 | |
| α-helix | 198-218 | 21 | |
| α-helix | 223-225 | 3 | |
| β-strand | 227-228 | 2 | 1 |
| α-helix | 230-232 | 3 | |
| α-helix | 245-257 | 13 | |
| β-strand | 266-269 | 4 | 1 |
| α-helix | 276-288 | 13 | |
| β-strand | 296-301 | 6 | 1 |
| α-helix | 303-313 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 320-337 | 18 | |
| α-helix | 360-362 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-22 | 14 | |
| β-strand | 28-32 | 5 | 5 |
| α-helix | 36-44 | 9 | |
| α-helix | 52-63 | 12 | |
| α-helix | 67-69 | 3 | |
| β-strand | 73-78 | 6 | 5 |
| α-helix | 80-83 | 4 | |
| β-strand | 86 | 1 | 6 |
| β-strand | 92 | 1 | 6 |
| α-helix | 93-99 | 7 | |
| α-helix | 102 | 1 | |
| β-strand | 103-107 | 5 | 5 |
| β-strand | 112-114 | 3 | 7 |
| β-strand | 122-124 | 3 | 7 |
| α-helix | 130-139 | 10 | |
| β-strand | 144-151 | 8 | 5 |
| β-strand | 154 | 1 | 8 |
| β-strand | 157 | 1 | 8 |
| α-helix | 160-179 | 20 | |
| β-strand | 183-190 | 8 | 5 |
| α-helix | 198-218 | 21 | |
| α-helix | 223-225 | 3 | |
| β-strand | 227-228 | 2 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 245-257 | 13 | |
| β-strand | 266-269 | 4 | 5 |
| α-helix | 276-288 | 13 | |
| β-strand | 296-301 | 6 | 5 |
| α-helix | 303-313 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 320-337 | 18 | |
| α-helix | 360-362 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-22 | 14 | |
| β-strand | 28-32 | 5 | 13 |
| α-helix | 36-44 | 9 | |
| α-helix | 52-63 | 12 | |
| α-helix | 67-69 | 3 | |
| β-strand | 73-78 | 6 | 13 |
| α-helix | 80-83 | 4 | |
| β-strand | 86 | 1 | 14 |
| β-strand | 92 | 1 | 14 |
| α-helix | 93-99 | 7 | |
| α-helix | 102 | 1 | |
| β-strand | 103-107 | 5 | 13 |
| β-strand | 112-114 | 3 | 15 |
| β-strand | 122-124 | 3 | 15 |
| α-helix | 130-139 | 10 | |
| β-strand | 142-151 | 10 | 13 |
| α-helix | 160-179 | 20 | |
| β-strand | 183-190 | 8 | 13 |
| α-helix | 198-218 | 21 | |
| α-helix | 223-225 | 3 | |
| β-strand | 227-228 | 2 | 13 |
| α-helix | 230-232 | 3 | |
| α-helix | 245-257 | 13 | |
| β-strand | 266-269 | 4 | 13 |
| α-helix | 276-288 | 13 | |
| β-strand | 296-301 | 6 | 13 |
| α-helix | 303-313 | 11 | |
| α-helix | 317-319 | 3 | |
| α-helix | 320-337 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fructose-bisphosphate aldolase A | A, B, C, D | protein | 363 | Oryctolagus cuniculus | P00883 (AlphaFold model) |
>5TLZ_1 Fructose-bisphosphate aldolase A (chains A, B, C, D) PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQ LLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNG ETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQN GIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT QKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFS YGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISN HAY
| ID | Name | Formula | Copies |
|---|---|---|---|
| N26 | naphthalene-2,6-diyl bis[dihydrogen (phosphate)] | C10 H10 O8 P2 | 4 |
Water and common crystallization additives (GOL) are not listed.
Bisphosphonate Inhibitors of Mammalian Glycolytic Aldolase. Heron, P.W., Abellan-Flos, M., Salmon, L. et al. J Med Chem (2018) 61:10558-10572. DOI 10.1021/acs.jmedchem.8b01000 · PubMed
Other PDB entries of the same protein (UniProt P00883 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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