The 2.7 Å resolution model of ovine cox-1 complexed with alclofenac. Determined by X-ray diffraction at 2.69 Å resolution. Released 11 Apr 2001.
Explore 1HT8 in 3D Show helices and sheets RCSB PDB PDBe
1HT8 contains 90 α-helices and 63 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 | 35-38 | 4 | |
| α-helix | 45 | 1 | |
| 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 | 84-85 | 2 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-104 | 8 | |
| 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 |
| α-helix | 153-156 | 4 | |
| β-strand | 161 | 1 | 6 |
| β-strand | 164 | 1 | 6 |
| α-helix | 171-173 | 3 | |
| α-helix | 174-181 | 8 | |
| β-strand | 183 | 1 | 7 |
| β-strand | 189 | 1 | 8 |
| β-strand | 194 | 1 | 9 |
| β-strand | 195 | 1 | 10 |
| α-helix | 196-206 | 11 | |
| β-strand | 212 | 1 | 11 |
| β-strand | 220 | 1 | 4 |
| β-strand | 221 | 1 | 11 |
| α-helix | 231-234 | 4 | |
| 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 |
| β-strand | 265 | 1 | 14 |
| α-helix | 281-283 | 3 | |
| α-helix | 284 | 1 | |
| β-strand | 285 | 1 | 14 |
| α-helix | 286 | 1 | |
| α-helix | 292-294 | 3 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-343 | 19 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-353 | 5 | |
| α-helix | 363-366 | 4 | |
| β-strand | 378 | 1 | 5 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-390 | 3 | |
| β-strand | 395-397 | 3 | 15 |
| β-strand | 400-402 | 3 | 15 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-428 | 16 | |
| β-strand | 430 | 1 | 10 |
| α-helix | 431 | 1 | |
| β-strand | 432 | 1 | 8 |
| α-helix | 433 | 1 | |
| β-strand | 440 | 1 | 7 |
| α-helix | 442-444 | 3 | |
| α-helix | 445-457 | 13 | |
| α-helix | 460-462 | 3 | |
| α-helix | 463-469 | 7 | |
| α-helix | 473-475 | 3 | |
| α-helix | 478-481 | 4 | |
| α-helix | 486-495 | 10 | |
| α-helix | 498-500 | 3 | |
| α-helix | 503-509 | 7 | |
| α-helix | 511-513 | 3 | |
| α-helix | 520-535 | 16 | |
| α-helix | 538-540 | 3 | |
| α-helix | 547-550 | 4 | |
| α-helix | 553-560 | 8 | |
| α-helix | 564-569 | 6 | |
| β-strand | 581 | 1 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 35-38 | 4 | |
| α-helix | 45 | 1 | |
| β-strand | 46-50 | 5 | 16 |
| β-strand | 54-58 | 5 | 16 |
| β-strand | 64-65 | 2 | 17 |
| β-strand | 71-72 | 2 | 17 |
| α-helix | 74-82 | 9 | |
| α-helix | 83-85 | 3 | |
| α-helix | 86-93 | 8 | |
| α-helix | 97-103 | 7 | |
| α-helix | 107-121 | 15 | |
| β-strand | 130-131 | 2 | 18 |
| α-helix | 139-143 | 5 | |
| β-strand | 147 | 1 | 19 |
| β-strand | 149-150 | 2 | 18 |
| α-helix | 153-156 | 4 | |
| β-strand | 161 | 1 | 20 |
| β-strand | 164 | 1 | 20 |
| α-helix | 174-181 | 8 | |
| β-strand | 183 | 1 | 21 |
| β-strand | 189 | 1 | 22 |
| β-strand | 194 | 1 | 23 |
| β-strand | 195 | 1 | 24 |
| α-helix | 196-206 | 11 | |
| β-strand | 212 | 1 | 25 |
| β-strand | 220 | 1 | 19 |
| β-strand | 221 | 1 | 25 |
| α-helix | 231-234 | 4 | |
| α-helix | 238-244 | 7 | |
| β-strand | 245 | 1 | 26 |
| α-helix | 251 | 1 | |
| β-strand | 252 | 1 | 26 |
| α-helix | 253 | 1 | |
| β-strand | 255-257 | 3 | 27 |
| β-strand | 260-262 | 3 | 27 |
| α-helix | 263-264 | 2 | |
| β-strand | 265 | 1 | 28 |
| α-helix | 281-283 | 3 | |
| β-strand | 285 | 1 | 28 |
| α-helix | 292-294 | 3 | |
| α-helix | 296-319 | 24 | |
| α-helix | 325-343 | 19 | |
| α-helix | 344-349 | 6 | |
| α-helix | 350-353 | 4 | |
| α-helix | 363-366 | 4 | |
| β-strand | 378 | 1 | 18 |
| α-helix | 379-384 | 6 | |
| α-helix | 388-390 | 3 | |
| β-strand | 395-397 | 3 | 29 |
| β-strand | 400-402 | 3 | 29 |
| α-helix | 404-407 | 4 | |
| α-helix | 413-428 | 16 | |
| β-strand | 430 | 1 | 24 |
| α-helix | 431 | 1 | |
| β-strand | 432 | 1 | 22 |
| α-helix | 433 | 1 | |
| β-strand | 440 | 1 | 21 |
| α-helix | 445-458 | 14 | |
| α-helix | 460-461 | 2 | |
| β-strand | 462 | 1 | 30 |
| α-helix | 463-469 | 7 | |
| α-helix | 473-475 | 3 | |
| α-helix | 478-481 | 4 | |
| α-helix | 486-495 | 10 | |
| α-helix | 498-500 | 3 | |
| β-strand | 502 | 1 | 30 |
| α-helix | 503-509 | 7 | |
| α-helix | 511 | 1 | |
| β-strand | 512 | 1 | 31 |
| α-helix | 513 | 1 | |
| β-strand | 519 | 1 | 31 |
| 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 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prostaglandin H2 synthase-1 | A, B | protein | 551 | Ovis aries | P05979 (AlphaFold model) |
>1HT8_1 PROSTAGLANDIN H2 SYNTHASE-1 (chains A, B) VNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHFL LTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRIL PSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKT SGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVL MHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQTA RLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMP DSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVI KESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKC HPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLNT KTCPYVSFHVP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 8 |
| BOG | octyl beta-D-glucopyranoside | C14 H28 O6 | 3 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 2 |
| 34C | (3-chloro-4-propoxy-phenyl)-acetic acid | C11 H13 Cl O3 | 2 |
Structural analysis of NSAID binding by prostaglandin H2 synthase: time-dependent and time-independent inhibitors elicit identical enzyme conformations. Selinsky, B.S., Gupta, K., Sharkey, C.T. et al. Biochemistry (2001) 40:5172-5180. DOI 10.1021/bi010045s · PubMed
Other PDB entries of the same protein (UniProt P05979 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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