Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PH9

The structure of Ibuprofen bound to cyclooxygenase-2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001516	biological_process	prostaglandin biosynthetic process
A	0004601	molecular_function	peroxidase activity
A	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005637	cellular_component	nuclear inner membrane
A	0005640	cellular_component	nuclear outer membrane
A	0005737	cellular_component	cytoplasm
A	0005783	cellular_component	endoplasmic reticulum
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006979	biological_process	response to oxidative stress
A	0007566	biological_process	embryo implantation
A	0008015	biological_process	blood circulation
A	0008217	biological_process	regulation of blood pressure
A	0009624	biological_process	response to nematode
A	0010269	biological_process	response to selenium ion
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0019371	biological_process	cyclooxygenase pathway
A	0019899	molecular_function	enzyme binding
A	0020037	molecular_function	heme binding
A	0030216	biological_process	keratinocyte differentiation
A	0030282	biological_process	bone mineralization
A	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
A	0031622	biological_process	positive regulation of fever generation
A	0032310	biological_process	prostaglandin secretion
A	0042127	biological_process	regulation of cell population proliferation
A	0042803	molecular_function	protein homodimerization activity
A	0043005	cellular_component	neuron projection
A	0043066	biological_process	negative regulation of apoptotic process
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046457	biological_process	prostanoid biosynthetic process
A	0046697	biological_process	decidualization
A	0046872	molecular_function	metal ion binding
A	0050873	biological_process	brown fat cell differentiation
A	0051213	molecular_function	dioxygenase activity
A	0071456	biological_process	cellular response to hypoxia
A	0071471	biological_process	cellular response to non-ionic osmotic stress
A	0071498	biological_process	cellular response to fluid shear stress
A	0090336	biological_process	positive regulation of brown fat cell differentiation
A	0098869	biological_process	cellular oxidant detoxification
A	0150077	biological_process	regulation of neuroinflammatory response
A	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
B	0001516	biological_process	prostaglandin biosynthetic process
B	0004601	molecular_function	peroxidase activity
B	0004666	molecular_function	prostaglandin-endoperoxide synthase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005637	cellular_component	nuclear inner membrane
B	0005640	cellular_component	nuclear outer membrane
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0006979	biological_process	response to oxidative stress
B	0007566	biological_process	embryo implantation
B	0008015	biological_process	blood circulation
B	0008217	biological_process	regulation of blood pressure
B	0009624	biological_process	response to nematode
B	0010269	biological_process	response to selenium ion
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0016702	molecular_function	oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0019371	biological_process	cyclooxygenase pathway
B	0019899	molecular_function	enzyme binding
B	0020037	molecular_function	heme binding
B	0030216	biological_process	keratinocyte differentiation
B	0030282	biological_process	bone mineralization
B	0031394	biological_process	positive regulation of prostaglandin biosynthetic process
B	0031622	biological_process	positive regulation of fever generation
B	0032310	biological_process	prostaglandin secretion
B	0042127	biological_process	regulation of cell population proliferation
B	0042803	molecular_function	protein homodimerization activity
B	0043005	cellular_component	neuron projection
B	0043066	biological_process	negative regulation of apoptotic process
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046457	biological_process	prostanoid biosynthetic process
B	0046697	biological_process	decidualization
B	0046872	molecular_function	metal ion binding
B	0050873	biological_process	brown fat cell differentiation
B	0051213	molecular_function	dioxygenase activity
B	0071456	biological_process	cellular response to hypoxia
B	0071471	biological_process	cellular response to non-ionic osmotic stress
B	0071498	biological_process	cellular response to fluid shear stress
B	0090336	biological_process	positive regulation of brown fat cell differentiation
B	0098869	biological_process	cellular oxidant detoxification
B	0150077	biological_process	regulation of neuroinflammatory response
B	1902219	biological_process	negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00298, ECO:0000269\|PubMed:20463020

Chain	Residue	Details
A	HIS208
B	HIS208

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: For cyclooxygenase activity => ECO:0000269\|PubMed:20463020

Chain	Residue	Details
A	TYR386
B	TYR386

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:20463020, ECO:0007744\|PDB:3KRK

Chain	Residue	Details
A	ARG121
A	TYR356
B	ARG121
B	TYR356

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: axial binding residue => ECO:0000269\|PubMed:12925531, ECO:0000269\|PubMed:20463020, ECO:0000269\|PubMed:20810665, ECO:0000269\|PubMed:21489986, ECO:0000269\|PubMed:8967954, ECO:0007744\|PDB:1CX2, ECO:0007744\|PDB:1PXX, ECO:0007744\|PDB:3LN0, ECO:0007744\|PDB:3LN1, ECO:0007744\|PDB:3MQE, ECO:0007744\|PDB:3NTB, ECO:0007744\|PDB:3NTG, ECO:0007744\|PDB:3PGH, ECO:0007744\|PDB:4COX, ECO:0007744\|PDB:4FM5, ECO:0007744\|PDB:4M10, ECO:0007744\|PDB:4M11, ECO:0007744\|PDB:4PH9, ECO:0007744\|PDB:5COX, ECO:0007744\|PDB:6COX

Chain	Residue	Details
A	HIS389
B	HIS389

site_id	SWS_FT_FI5
Number of Residues	2
Details	SITE: Aspirin-acetylated serine

Chain	Residue	Details
A	SER531
B	SER531

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250\|UniProtKB:P35354

Chain	Residue	Details
A	CYS541
B	CYS541

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: O-acetylserine; by SPHK1 => ECO:0000269\|PubMed:29662056

Chain	Residue	Details
A	SER580
B	SER580

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10811226, ECO:0000269\|PubMed:12925531, ECO:0000269\|PubMed:20463020, ECO:0000269\|PubMed:20810665, ECO:0000269\|PubMed:21467029, ECO:0000269\|PubMed:21489986, ECO:0000269\|PubMed:8349699, ECO:0000269\|PubMed:8967954, ECO:0007744\|PDB:1CVU, ECO:0007744\|PDB:1CX2, ECO:0007744\|PDB:1DDX, ECO:0007744\|PDB:1PXX, ECO:0007744\|PDB:3HS5, ECO:0007744\|PDB:3HS6, ECO:0007744\|PDB:3HS7, ECO:0007744\|PDB:3KRK, ECO:0007744\|PDB:3LN0, ECO:0007744\|PDB:3LN1, ECO:0007744\|PDB:3MDL, ECO:0007744\|PDB:3MQE, ECO:0007744\|PDB:3NT1, ECO:0007744\|PDB:3NTB, ECO:0007744\|PDB:3PGH, ECO:0007744\|PDB:3QH0, ECO:0007744\|PDB:3QMO, ECO:0007744\|PDB:3TZI, ECO:0007744\|PDB:4COX, ECO:0007744\|PDB:4E1G, ECO:0007744\|PDB:4M10, ECO:0007744\|PDB:4M11, ECO:0007744\|PDB:4OTJ, ECO:0007744\|PDB:4OTY, ECO:0007744\|PDB:4PH9, ECO:0007744\|PDB:4RRW, ECO:0007744\|PDB:4RRX, ECO:0007744\|PDB:4RRY, ECO:0007744\|PDB:4RRZ, ECO:0007744\|PDB:4RS0, ECO:0007744\|PDB:4RUT, ECO:0007744\|PDB:4Z0L, ECO:0007744\|PDB:5COX, ECO:0007744\|PDB:5FDQ, ECO:0007744\|PDB:5JVY, ECO:0007744\|PDB:5JVZ, ECO:0007744\|PDB:5JW1, ECO:0007744\|PDB:6COX

Chain	Residue	Details
A	ASN68
B	ASN68

site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10811226, ECO:0000269\|PubMed:12925531, ECO:0000269\|PubMed:20463020, ECO:0000269\|PubMed:20810665, ECO:0000269\|PubMed:21467029, ECO:0000269\|PubMed:21489986, ECO:0000269\|PubMed:8349699, ECO:0000269\|PubMed:8967954, ECO:0007744\|PDB:1CVU, ECO:0007744\|PDB:1CX2, ECO:0007744\|PDB:1DDX, ECO:0007744\|PDB:1PXX, ECO:0007744\|PDB:3HS5, ECO:0007744\|PDB:3HS6, ECO:0007744\|PDB:3HS7, ECO:0007744\|PDB:3KRK, ECO:0007744\|PDB:3LN0, ECO:0007744\|PDB:3LN1, ECO:0007744\|PDB:3MDL, ECO:0007744\|PDB:3MQE, ECO:0007744\|PDB:3NT1, ECO:0007744\|PDB:3NTB, ECO:0007744\|PDB:3NTG, ECO:0007744\|PDB:3OLT, ECO:0007744\|PDB:3OLU, ECO:0007744\|PDB:3PGH, ECO:0007744\|PDB:3QH0, ECO:0007744\|PDB:3QMO, ECO:0007744\|PDB:3TZI, ECO:0007744\|PDB:4COX, ECO:0007744\|PDB:4E1G, ECO:0007744\|PDB:4FM5, ECO:0007744\|PDB:4M10, ECO:0007744\|PDB:4M11, ECO:0007744\|PDB:4OTJ, ECO:0007744\|PDB:4OTY, ECO:0007744\|PDB:4PH9, ECO:0007744\|PDB:4RRW, ECO:0007744\|PDB:4RRX, ECO:0007744\|PDB:4RRY, ECO:0007744\|PDB:4RRZ, ECO:0007744\|PDB:4RS0, ECO:0007744\|PDB:4RUT, ECO:0007744\|PDB:4Z0L, ECO:0007744\|PDB:5COX, ECO:0007744\|PDB:5FDQ, ECO:0007744\|PDB:5JVY, ECO:0007744\|PDB:5JVZ, ECO:0007744\|PDB:5JW1, ECO:0007744\|PDB:6COX

Chain	Residue	Details
A	ASN145
B	ASN145

site_id	SWS_FT_FI10
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:10811226, ECO:0000269\|PubMed:12925531, ECO:0000269\|PubMed:20463020, ECO:0000269\|PubMed:20810665, ECO:0000269\|PubMed:21467029, ECO:0000269\|PubMed:21489986, ECO:0000269\|PubMed:8349699, ECO:0000269\|PubMed:8967954, ECO:0007744\|PDB:1CVU, ECO:0007744\|PDB:1CX2, ECO:0007744\|PDB:1DDX, ECO:0007744\|PDB:1PXX, ECO:0007744\|PDB:3HS5, ECO:0007744\|PDB:3HS6, ECO:0007744\|PDB:3HS7, ECO:0007744\|PDB:3KRK, ECO:0007744\|PDB:3LN0, ECO:0007744\|PDB:3LN1, ECO:0007744\|PDB:3MDL, ECO:0007744\|PDB:3MQE, ECO:0007744\|PDB:3NT1, ECO:0007744\|PDB:3NTB, ECO:0007744\|PDB:3NTG, ECO:0007744\|PDB:3OLT, ECO:0007744\|PDB:3OLU, ECO:0007744\|PDB:3PGH, ECO:0007744\|PDB:3QH0, ECO:0007744\|PDB:3QMO, ECO:0007744\|PDB:3TZI, ECO:0007744\|PDB:4COX, ECO:0007744\|PDB:4E1G, ECO:0007744\|PDB:4M10, ECO:0007744\|PDB:4M11, ECO:0007744\|PDB:4OTJ, ECO:0007744\|PDB:4OTY, ECO:0007744\|PDB:4PH9, ECO:0007744\|PDB:4RRW, ECO:0007744\|PDB:4RRX, ECO:0007744\|PDB:4RRY, ECO:0007744\|PDB:4RRZ, ECO:0007744\|PDB:4RS0, ECO:0007744\|PDB:4RUT, ECO:0007744\|PDB:4Z0L, ECO:0007744\|PDB:5COX, ECO:0007744\|PDB:5FDQ, ECO:0007744\|PDB:5JVY, ECO:0007744\|PDB:5JVZ, ECO:0007744\|PDB:5JW1, ECO:0007744\|PDB:6COX

Chain	Residue	Details
A	ASN411
B	ASN411

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 37

Chain	Residue	Details
A	GLN204	electrostatic stabiliser, hydrogen bond donor
A	HIS208	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	LEU385	steric role
A	TYR386	hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser
A	HIS389	metal ligand
A	GLY527	steric role
A	SER531	electrostatic stabiliser

site_id	MCSA2
Number of Residues	7
Details	M-CSA 37

Chain	Residue	Details
B	GLN204	electrostatic stabiliser, hydrogen bond donor
B	HIS208	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	LEU385	steric role
B	TYR386	hydrogen bond acceptor, hydrogen bond donor, hydrogen radical acceptor, hydrogen radical donor, radical stabiliser
B	HIS389	metal ligand
B	GLY527	steric role
B	SER531	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)