Structure of E. Coli alkaline phosphatase inhibited by the inorganic phosphate at 1.75A resolution. Determined by X-ray diffraction at 1.75 Å resolution. Released 20 Sept 2000.
Explore 1ED8 in 3D Show helices and sheets RCSB PDB PDBe
1ED8 contains 48 α-helices and 57 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 | 30-34 | 5 | |
| α-helix | 41-42 | 2 | |
| β-strand | 44-50 | 7 | 1 |
| α-helix | 55-65 | 11 | |
| β-strand | 80-85 | 6 | 1 |
| β-strand | 88-89 | 2 | 2 |
| β-strand | 96-97 | 2 | 2 |
| α-helix | 102-111 | 10 | |
| β-strand | 116 | 1 | 2 |
| β-strand | 120 | 1 | 3 |
| β-strand | 122 | 1 | 4 |
| β-strand | 128 | 1 | 4 |
| α-helix | 132-138 | 7 | |
| β-strand | 142-150 | 9 | 1 |
| α-helix | 154-157 | 4 | |
| β-strand | 163 | 1 | 3 |
| α-helix | 171-177 | 7 | |
| α-helix | 183-185 | 3 | |
| α-helix | 191-198 | 8 | |
| β-strand | 202-206 | 5 | 1 |
| α-helix | 209-212 | 4 | |
| β-strand | 214 | 1 | 5 |
| β-strand | 215 | 1 | 6 |
| β-strand | 221 | 1 | 6 |
| β-strand | 224 | 1 | 5 |
| α-helix | 225-231 | 7 | |
| α-helix | 234 | 1 | |
| β-strand | 235-237 | 3 | 1 |
| α-helix | 240-245 | 6 | |
| β-strand | 255-258 | 4 | 1 |
| α-helix | 264-266 | 3 | |
| β-strand | 268-269 | 2 | 7 |
| α-helix | 271-273 | 3 | |
| β-strand | 274-275 | 2 | 8 |
| α-helix | 277-280 | 4 | |
| α-helix | 282-283 | 2 | |
| β-strand | 284 | 1 | 8 |
| β-strand | 287-288 | 2 | 7 |
| α-helix | 299-311 | 13 | |
| β-strand | 317-323 | 7 | 1 |
| α-helix | 325-331 | 7 | |
| α-helix | 335-359 | 25 | |
| β-strand | 362-367 | 6 | 1 |
| β-strand | 371 | 1 | 9 |
| β-strand | 375-377 | 3 | 8 |
| β-strand | 386-391 | 6 | 8 |
| β-strand | 397-402 | 6 | 8 |
| α-helix | 410-412 | 3 | |
| β-strand | 413 | 1 | 9 |
| β-strand | 417-422 | 6 | 1 |
| α-helix | 426-429 | 4 | |
| β-strand | 431-434 | 4 | 1 |
| α-helix | 435-446 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 530-534 | 5 | |
| α-helix | 541-542 | 2 | |
| β-strand | 544-550 | 7 | 1 |
| α-helix | 555-565 | 11 | |
| α-helix | 575-577 | 3 | |
| β-strand | 580-585 | 6 | 1 |
| β-strand | 588-589 | 2 | 10 |
| β-strand | 596-597 | 2 | 10 |
| α-helix | 602-611 | 10 | |
| β-strand | 620 | 1 | 11 |
| β-strand | 622 | 1 | 12 |
| β-strand | 628 | 1 | 12 |
| α-helix | 632-638 | 7 | |
| β-strand | 642-650 | 9 | 1 |
| α-helix | 654-657 | 4 | |
| β-strand | 663 | 1 | 11 |
| α-helix | 671-677 | 7 | |
| α-helix | 679-681 | 3 | |
| α-helix | 683-685 | 3 | |
| α-helix | 691-698 | 8 | |
| β-strand | 702-706 | 5 | 1 |
| α-helix | 708-712 | 5 | |
| β-strand | 714 | 1 | 13 |
| β-strand | 724 | 1 | 13 |
| α-helix | 725-731 | 7 | |
| β-strand | 735-737 | 3 | 1 |
| α-helix | 740-745 | 6 | |
| β-strand | 755-758 | 4 | 1 |
| α-helix | 764-766 | 3 | |
| β-strand | 768-769 | 2 | 14 |
| α-helix | 771-773 | 3 | |
| β-strand | 774-775 | 2 | 15 |
| α-helix | 777-780 | 4 | |
| α-helix | 782-783 | 2 | |
| β-strand | 784 | 1 | 15 |
| β-strand | 787-788 | 2 | 14 |
| α-helix | 797-798 | 2 | |
| α-helix | 799-811 | 13 | |
| β-strand | 817-823 | 7 | 1 |
| α-helix | 825-831 | 7 | |
| α-helix | 835-859 | 25 | |
| β-strand | 862-868 | 7 | 1 |
| β-strand | 871 | 1 | 16 |
| β-strand | 875-877 | 3 | 15 |
| β-strand | 886-891 | 6 | 15 |
| β-strand | 897-902 | 6 | 15 |
| α-helix | 910-912 | 3 | |
| β-strand | 913 | 1 | 16 |
| β-strand | 917-922 | 6 | 1 |
| α-helix | 926-929 | 4 | |
| β-strand | 931-934 | 4 | 1 |
| α-helix | 935-946 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alkaline phosphatase | A, B | protein | 449 | Escherichia coli | P00634 (AlphaFold model) |
>1ED8_1 ALKALINE PHOSPHATASE (chains A, B) TPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITA ARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGAL GVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPG NALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDA ASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLA QMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEG NTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIA AYGPHAANVVGLTDQTDLFYTMKAALGLK
Water and common crystallization additives (SO4) are not listed.
A revised mechanism for the alkaline phosphatase reaction involving three metal ions. Stec, B., Holtz, K.M., Kantrowitz, E.R. J Mol Biol (2000) 299:1303-1311. DOI 10.1006/jmbi.2000.3799 · PubMed
Other PDB entries of the same protein (UniProt P00634 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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