1EQH: The 2.7 Å model of ovine cox-1

The 2.7 Å model of ovine cox-1 complexed with flurbiprofen. Determined by X-ray diffraction at 2.7 Å resolution. Released 11 Apr 2001.

Method
X-ray diffraction
Resolution
2.7 Å
Organism
Ovis aries
Chains
2
Atoms
9,530
Mol. weight
138 kDa
Ligands
NAG, BOG, HEM, FLP
Released
11 Apr 2001

Explore 1EQH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EQH contains 91 α-helices and 60 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.

Chain A: 45 helices, 31 β-strands

ElementResiduesLengthSheet
α-helix35-384
α-helix451
β-strand46-5051
β-strand54-5851
β-strand64-6522
β-strand71-7222
α-helix74-829
α-helix84-852
α-helix86-938
α-helix97-1037
α-helix107-12115
β-strand130-13123
α-helix139-1435
β-strand14714
β-strand149-15023
α-helix153-1564
β-strand16115
β-strand16415
α-helix171-1733
α-helix174-1818
β-strand18316
β-strand18917
β-strand19418
β-strand19519
α-helix196-20611
β-strand212110
β-strand22014
β-strand221110
α-helix231-2344
α-helix238-2447
β-strand245111
α-helix2511
β-strand252111
α-helix2531
β-strand255-257312
β-strand260-262312
α-helix263-2642
β-strand265113
α-helix281-2833
β-strand285113
α-helix290-2945
α-helix296-31924
α-helix325-34319
α-helix344-3485
α-helix349-3535
α-helix363-3664
β-strand37813
α-helix379-3846
α-helix388-3903
β-strand395-397314
β-strand400-402314
α-helix404-4074
α-helix413-42816
β-strand43019
α-helix4311
β-strand43217
α-helix4331
β-strand44016
α-helix442-4443
α-helix445-45713
α-helix460-4612
β-strand462115
α-helix463-4697
α-helix473-4753
α-helix478-4814
α-helix486-49510
α-helix498-5003
β-strand502115
α-helix503-5097
α-helix511-5133
α-helix520-53516
α-helix538-5403
α-helix547-5504
α-helix553-5608
α-helix564-5696
β-strand58118
Chain B: 46 helices, 29 β-strands
ElementResiduesLengthSheet
α-helix35-384
β-strand46-50516
β-strand54-58516
β-strand64-65217
β-strand71-72217
α-helix74-829
α-helix84-852
α-helix86-938
α-helix97-1048
α-helix108-12114
β-strand130-131218
α-helix139-1435
β-strand147119
β-strand149-150218
α-helix153-1553
β-strand161120
β-strand164120
α-helix171-1733
α-helix174-1818
β-strand183121
β-strand189122
β-strand194123
β-strand195124
α-helix196-20611
β-strand212125
β-strand220119
β-strand221125
α-helix231-2344
α-helix238-2447
β-strand245126
α-helix2511
β-strand252126
α-helix2531
β-strand255-257327
β-strand260-262327
α-helix263-2642
β-strand265128
α-helix281-2833
α-helix2841
β-strand285128
α-helix2861
α-helix292-2943
α-helix296-31924
α-helix325-34319
α-helix344-3485
α-helix349-3535
α-helix363-3664
β-strand378118
α-helix379-3846
α-helix388-3903
β-strand395-397329
β-strand400-402329
α-helix404-4074
α-helix413-42816
β-strand430124
α-helix4311
β-strand432122
α-helix4331
β-strand440121
α-helix442-4443
α-helix445-45713
α-helix460-4623
α-helix463-4697
α-helix473-4753
α-helix478-4814
α-helix486-49510
α-helix498-5003
α-helix503-5097
α-helix511-5133
α-helix520-53516
α-helix538-5403
α-helix547-5504
α-helix553-5608
α-helix564-5696
β-strand581123

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Prostaglandin H2 synthase-1A, Bprotein580Ovis ariesP05979 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1EQH_1 PROSTAGLANDIN H2 SYNTHASE-1 (chains A, B)
PVFSADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRT
TLRPSPSFIHFLLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWE
SFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAF
FAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGE
VYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEH
PTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAME
FNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNI
DHHILHVAVDVIKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDA
LEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVK
TATLKKLVCLNTKTCPYVSFHVPDPRQEDRPGVERPPTEL

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O610
BOGoctyl beta-D-glucopyranosideC14 H28 O63
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O42
FLPFlurbiprofenC15 H13 F O22

Primary citation

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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