3KK6: Cyclooxygenase-1

Crystal Structure of Cyclooxygenase-1 in complex with celecoxib. Determined by X-ray diffraction at 2.75 Å resolution. Released 15 Dec 2009.

Method: X-ray diffraction
Resolution: 2.75 Å
Organism: Ovis aries
Chains: 2
Atoms: 9,372
Mol. weight: 133.74 kDa
Ligands: BOG, FLC, CEL, HEM
Released: 15 Dec 2009

Explore 3KK6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3KK6 contains 72 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: 35 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	35-37	3
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	73	1
α-helix	74-81	8
α-helix	86-92	7
α-helix	97-103	7
α-helix	108-121	14
β-strand	130-131	2	3
β-strand	134	1	3
α-helix	139-143	5
β-strand	147	1	4
β-strand	149-150	2	3
β-strand	161	1	5
β-strand	164	1	5
α-helix	171-173	3
α-helix	174-178	5
β-strand	183	1	6
β-strand	189	1	7
β-strand	194	1	8
β-strand	195	1	9
α-helix	196-206	11
β-strand	212	1	10
β-strand	220	1	4
β-strand	221	1	10
α-helix	238-244	7
β-strand	245	1	11
β-strand	252	1	11
β-strand	255-257	3	12
β-strand	260-262	3	12
α-helix	263-264	2
β-strand	265	1	13
α-helix	275-276	2
β-strand	285	1	13
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	3
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	420-426	7
β-strand	430	1	9
β-strand	432	1	7
β-strand	440	1	6
α-helix	445-458	14
α-helix	463-469	7
α-helix	473-475	3
α-helix	478-482	5
α-helix	485-494	10
α-helix	498-500	3
α-helix	503-509	7
α-helix	520-535	16
α-helix	538-540	3
α-helix	548-550	3
α-helix	553-560	8
α-helix	566-569	4
β-strand	581	1	8

Chain B: 37 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	35-38	4
β-strand	46-50	5	15
β-strand	54-58	5	15
β-strand	64-65	2	16
β-strand	71-72	2	16
α-helix	73	1
α-helix	74-81	8
α-helix	86-92	7
α-helix	97-103	7
α-helix	108-121	14
β-strand	130-131	2	17
β-strand	134	1	17
α-helix	139-143	5
β-strand	147	1	18
α-helix	148	1
β-strand	149-150	2	17
α-helix	153-156	4
β-strand	161	1	19
β-strand	164	1	19
α-helix	171-173	3
α-helix	174-178	5
β-strand	183	1	20
β-strand	189	1	21
β-strand	194	1	22
β-strand	195	1	23
α-helix	196-206	11
β-strand	212	1	24
β-strand	220	1	18
β-strand	221	1	24
α-helix	238-244	7
β-strand	245	1	25
β-strand	252	1	25
β-strand	255-257	3	26
β-strand	260-262	3	26
α-helix	263-264	2
β-strand	265	1	27
α-helix	281-283	3
β-strand	285	1	27
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	17
α-helix	379-384	6
α-helix	388-390	3
β-strand	395-397	3	28
β-strand	400-402	3	28
α-helix	404-407	4
α-helix	413-417	5
α-helix	420-426	7
β-strand	430	1	23
β-strand	432	1	21
β-strand	440	1	20
α-helix	445-458	14
α-helix	463-469	7
α-helix	473-475	3
α-helix	478-482	5
α-helix	485-492	8
α-helix	498-500	3
α-helix	503-509	7
α-helix	520-535	16
α-helix	538-540	3
α-helix	548-550	3
α-helix	553-560	8
α-helix	566-569	4
β-strand	581	1	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Prostaglandin G/H synthase 1	A, B	protein	553	Ovis aries	P05979 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3KK6_1 Prostaglandin G/H synthase 1 (chains A, B)
PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHF
LLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRI
LPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFK
TSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPV
LMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQT
ARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLM
PDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDV
IKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEK
CHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLN
TKTCPYVSFHVPD

Ligands and cofactors

ID	Name	Formula	Copies
BOG	octyl beta-D-glucopyranoside	C14 H28 O6	4
FLC	Citrate anion	C6 H5 O7	1
CEL	4-[5-(4-methylphenyl)-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzenesulfonamide	C17 H14 F3 N3 O2 S	2
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	2

Primary citation

Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1. Rimon, G., Sidhu, R.S., Lauver, D.A. et al. Proc Natl Acad Sci U S A (2010) 107:28-33. DOI 10.1073/pnas.0909765106 · PubMed

Other PDB entries of the same protein (UniProt P05979 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1Q4G 2.0 Å, 2.0 Angstrom Crystal Structure of Ovine Prostaglandin H2 Synthase-1, in complex with…
2AYL 2.0 Å, 2.0 Angstrom Crystal Structure of Manganese Protoporphyrin IX-reconstituted Ovine…
4O1Z 2.4 Å, Crystal Structure of Ovine Cyclooxygenase-1 Complex with Meloxicam
3N8Y 2.6 Å, Structure of Aspirin Acetylated Cyclooxygenase-1 in Complex with Diclofenac
1EQG 2.61 Å, The 2.6 Å model of ovine cox-1 complexed with ibuprofen
1HT8 2.69 Å, The 2.7 Å resolution model of ovine cox-1 complexed with alclofenac
1EQH 2.7 Å, The 2.7 Å model of ovine cox-1 complexed with flurbiprofen
2OYU 2.7 Å, Indomethacin-(S)-alpha-ethyl-ethanolamide bound to Cyclooxygenase-1
1HT5 2.75 Å, The 2.75 Å resolution model of ovine cox-1 complexed with methyl ester flurbiprofen
3N8W 2.75 Å, Crystal Structure of R120Q/Native Cyclooxygenase-1 Heterodimer mutant in complex with…
3N8X 2.75 Å, Crystal Structure of Cyclooxygenase-1 in Complex with Nimesulide
5WBE 2.75 Å, Cox-1:MOFEZOLAC complex structure

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