Indomethacin-(S)-alpha-ethyl-ethanolamide bound to Cyclooxygenase-1. Determined by X-ray diffraction at 2.7 Å resolution. Released 24 Jul 2007.
Explore 2OYU in 3D Show helices and sheets RCSB PDB PDBe
2OYU contains 39 α-helices and 30 β-strands across 1 chain. 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 | 35-38 | 4 | |
| β-strand | 46-50 | 5 | 1 |
| β-strand | 54-58 | 5 | 1 |
| β-strand | 64-65 | 2 | 2 |
| β-strand | 71-72 | 2 | 2 |
| α-helix | 74-82 | 9 | |
| α-helix | 83-85 | 3 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-105 | 9 | |
| α-helix | 108-121 | 14 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 139-143 | 5 | |
| β-strand | 147 | 1 | 4 |
| β-strand | 149 | 1 | 5 |
| β-strand | 150 | 1 | 3 |
| β-strand | 154 | 1 | 6 |
| α-helix | 155-156 | 2 | |
| β-strand | 161 | 1 | 7 |
| β-strand | 164 | 1 | 7 |
| α-helix | 174-181 | 8 | |
| β-strand | 183 | 1 | 8 |
| β-strand | 189 | 1 | 9 |
| β-strand | 194 | 1 | 10 |
| α-helix | 196-206 | 11 | |
| β-strand | 212 | 1 | 11 |
| β-strand | 220 | 1 | 4 |
| β-strand | 221 | 1 | 11 |
| α-helix | 238-244 | 7 | |
| β-strand | 245 | 1 | 12 |
| α-helix | 251 | 1 | |
| β-strand | 252 | 1 | 12 |
| α-helix | 253 | 1 | |
| β-strand | 255-257 | 3 | 13 |
| β-strand | 260-262 | 3 | 13 |
| α-helix | 263-265 | 3 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-343 | 19 | |
| α-helix | 344-349 | 6 | |
| α-helix | 350-353 | 4 | |
| α-helix | 363-365 | 3 | |
| β-strand | 378 | 1 | 5 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-390 | 3 | |
| β-strand | 395-397 | 3 | 14 |
| β-strand | 400-402 | 3 | 14 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-417 | 5 | |
| α-helix | 419-428 | 10 | |
| β-strand | 432 | 1 | 9 |
| β-strand | 440 | 1 | 8 |
| α-helix | 445-457 | 13 | |
| β-strand | 460 | 1 | 6 |
| α-helix | 461-462 | 2 | |
| α-helix | 463-469 | 7 | |
| α-helix | 472-475 | 4 | |
| α-helix | 478-481 | 4 | |
| α-helix | 485-495 | 11 | |
| α-helix | 498-500 | 3 | |
| α-helix | 503-509 | 7 | |
| α-helix | 511 | 1 | |
| β-strand | 512 | 1 | 15 |
| α-helix | 513 | 1 | |
| β-strand | 519 | 1 | 15 |
| α-helix | 520-535 | 16 | |
| α-helix | 538-540 | 3 | |
| α-helix | 548-550 | 3 | |
| α-helix | 553-560 | 8 | |
| α-helix | 564-569 | 6 | |
| β-strand | 581 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prostaglandin G/H synthase 1 | P | protein | 600 | Ovis aries | P05979 (AlphaFold model) |
>2OYU_1 Prostaglandin G/H synthase 1 (chains P) MSRQSISLRFPLLLLLLSPSPVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCT RTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVR SNLIPSPPTYNIAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRR FLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLER QYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLML YATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLK FDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVE ALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQE LTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPIC SPEYWKASTFGGEVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 2 |
| IMS | 2-[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]-N-[(1S)-1-(hydroxymeth… | C23 H25 Cl N2 O4 | 1 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 1 |
Structural basis of enantioselective inhibition of cyclooxygenase-1 by S-alpha-substituted indomethacin ethanolamides. Harman, C.A., Turman, M.V., Kozak, K.R. et al. J Biol Chem (2007) 282:28096-28105. DOI 10.1074/jbc.M701335200 · PubMed
Other PDB entries of the same protein (UniProt P05979 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2OYU 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.