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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5IKV

The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0001516biological_processprostaglandin biosynthetic process
A0004601molecular_functionperoxidase activity
A0004666molecular_functionprostaglandin-endoperoxide synthase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005637cellular_componentnuclear inner membrane
A0005640cellular_componentnuclear outer membrane
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006693biological_processprostaglandin metabolic process
A0006979biological_processresponse to oxidative stress
A0007566biological_processembryo implantation
A0008217biological_processregulation of blood pressure
A0009624biological_processresponse to nematode
A0010269biological_processresponse to selenium ion
A0010575biological_processpositive regulation of vascular endothelial growth factor production
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0019371biological_processcyclooxygenase pathway
A0019372biological_processlipoxygenase pathway
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0031394biological_processpositive regulation of prostaglandin biosynthetic process
A0031622biological_processpositive regulation of fever generation
A0032310biological_processprostaglandin secretion
A0042127biological_processregulation of cell population proliferation
A0042759biological_processlong-chain fatty acid biosynthetic process
A0042803molecular_functionprotein homodimerization activity
A0043005cellular_componentneuron projection
A0043066biological_processnegative regulation of apoptotic process
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0046697biological_processdecidualization
A0046872molecular_functionmetal ion binding
A0050727biological_processregulation of inflammatory response
A0050873biological_processbrown fat cell differentiation
A0051213molecular_functiondioxygenase activity
A0071456biological_processcellular response to hypoxia
A0071471biological_processcellular response to non-ionic osmotic stress
A0071498biological_processcellular response to fluid shear stress
A0071636biological_processpositive regulation of transforming growth factor beta production
A0090050biological_processpositive regulation of cell migration involved in sprouting angiogenesis
A0090271biological_processpositive regulation of fibroblast growth factor production
A0090336biological_processpositive regulation of brown fat cell differentiation
A0090362biological_processpositive regulation of platelet-derived growth factor production
A0098869biological_processcellular oxidant detoxification
A0150077biological_processregulation of neuroinflammatory response
A1902219biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
B0001516biological_processprostaglandin biosynthetic process
B0004601molecular_functionperoxidase activity
B0004666molecular_functionprostaglandin-endoperoxide synthase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005637cellular_componentnuclear inner membrane
B0005640cellular_componentnuclear outer membrane
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0006693biological_processprostaglandin metabolic process
B0006979biological_processresponse to oxidative stress
B0007566biological_processembryo implantation
B0008217biological_processregulation of blood pressure
B0009624biological_processresponse to nematode
B0010269biological_processresponse to selenium ion
B0010575biological_processpositive regulation of vascular endothelial growth factor production
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016701molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0019371biological_processcyclooxygenase pathway
B0019372biological_processlipoxygenase pathway
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0031394biological_processpositive regulation of prostaglandin biosynthetic process
B0031622biological_processpositive regulation of fever generation
B0032310biological_processprostaglandin secretion
B0042127biological_processregulation of cell population proliferation
B0042759biological_processlong-chain fatty acid biosynthetic process
B0042803molecular_functionprotein homodimerization activity
B0043005cellular_componentneuron projection
B0043066biological_processnegative regulation of apoptotic process
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0046697biological_processdecidualization
B0046872molecular_functionmetal ion binding
B0050727biological_processregulation of inflammatory response
B0050873biological_processbrown fat cell differentiation
B0051213molecular_functiondioxygenase activity
B0071456biological_processcellular response to hypoxia
B0071471biological_processcellular response to non-ionic osmotic stress
B0071498biological_processcellular response to fluid shear stress
B0071636biological_processpositive regulation of transforming growth factor beta production
B0090050biological_processpositive regulation of cell migration involved in sprouting angiogenesis
B0090271biological_processpositive regulation of fibroblast growth factor production
B0090336biological_processpositive regulation of brown fat cell differentiation
B0090362biological_processpositive regulation of platelet-derived growth factor production
B0098869biological_processcellular oxidant detoxification
B0150077biological_processregulation of neuroinflammatory response
B1902219biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"For cyclooxygenase activity","evidences":[{"source":"UniProtKB","id":"Q05769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q05769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00298","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Aspirin-acetylated serine","evidences":[{"source":"PubMed","id":"26859324","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"16373578","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"O-acetylserine","evidences":[{"source":"UniProtKB","id":"Q05769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26859324","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27226593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26859324","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27226593","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27710942","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F19","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KIR","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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