4O1Z: Ovine Cyclooxygenase-1 Complex with Meloxicam

Crystal Structure of Ovine Cyclooxygenase-1 Complex with Meloxicam. Determined by X-ray diffraction at 2.4 Å resolution. Released 22 Jan 2014.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Ovis aries
Chains: 2
Atoms: 9,615
Mol. weight: 135.25 kDa
Ligands: MXM, NAG, HEM
Released: 22 Jan 2014

Explore 4O1Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4O1Z contains 87 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: 42 helices, 30 β-strands

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	97-103	7
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
α-helix	263-264	2
β-strand	265	1	14
α-helix	281-283	3
β-strand	285	1	14
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	413-417	5
α-helix	419-428	10
β-strand	430	1	10
β-strand	432	1	8
β-strand	440	1	7
α-helix	445-457	13
α-helix	460-462	3
α-helix	463-469	7
α-helix	473-475	3
α-helix	478-482	5
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

Chain B: 45 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	35-38	4
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	74-81	8
α-helix	86-93	8
α-helix	97-104	8
α-helix	108-121	14
β-strand	130	1	18
α-helix	139-143	5
β-strand	147	1	19
β-strand	149	1	20
β-strand	150	1	18
α-helix	153-156	4
β-strand	161	1	21
β-strand	164	1	21
α-helix	171-173	3
α-helix	174-181	8
β-strand	183	1	22
β-strand	189	1	23
β-strand	194	1	24
β-strand	195	1	25
α-helix	196-206	11
β-strand	212	1	26
β-strand	220	1	19
β-strand	221	1	26
α-helix	231-234	4
α-helix	238-244	7
β-strand	245	1	27
α-helix	251	1
β-strand	252	1	27
α-helix	253	1
β-strand	255-257	3	28
β-strand	260-262	3	28
α-helix	263-264	2
β-strand	265	1	29
α-helix	281-283	3
α-helix	284	1
β-strand	285	1	29
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	20
α-helix	379-384	6
α-helix	388-390	3
β-strand	395-397	3	30
β-strand	400-402	3	30
α-helix	404-407	4
α-helix	413-417	5
α-helix	419-428	10
β-strand	430	1	25
α-helix	431	1
β-strand	432	1	23
α-helix	433	1
β-strand	440	1	22
α-helix	445-457	13
α-helix	460-462	3
α-helix	463-469	7
α-helix	473-475	3
α-helix	478-482	5
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	548-550	3
α-helix	553-560	8
α-helix	564-569	6
β-strand	581	1	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Prostaglandin G/H synthase 1	A, B	protein	569	Ovis aries	P05979 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4O1Z_1 Prostaglandin G/H synthase 1 (chains A, B)
PVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPEIWTWLRTTLRPSPSFIHF
LLTHGRWLWDFVNATFIRDTLMRLVLTVRSNLIPSPPTYNIAHDYISWESFSNVSYYTRI
LPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFK
TSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPV
LMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATIWLREHNRVCDLLKAEHPTWGDEQLFQT
ARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLM
PDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDV
IKESRVLRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEK
CHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGEVGFNLVKTATLKKLVCLN
TKTCPYVSFHVPDPRQEDRPGVERPPTEL

Ligands and cofactors

ID	Name	Formula	Copies
MXM	4-hydroxy-2-methyl-N-(5-methyl-1,3-thiazol-2-yl)-2H-1,2-benzothiazine-3-carboxa…	C14 H13 N3 O4 S2	2
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	2

Primary citation

Oxicams Bind in a Novel Mode to the Cyclooxygenase Active Site via a Two-water-mediated H-bonding Network. Xu, S., Hermanson, D.J., Banerjee, S. et al. J Biol Chem (2014) 289:6799-6808. DOI 10.1074/jbc.M113.517987 · 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…
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
3KK6 2.75 Å, Crystal Structure of Cyclooxygenase-1 in complex with celecoxib
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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