Structure of PDB 3rr3 Chain A

Receptor sequence
>3rr3A (length=552) Species: 10090 (Mus musculus) [Search protein sequence]
ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLL
KPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYN
VHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKV
LLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPE
NLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQT
SRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEF
NTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEEL
TGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSL
KGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFN
VQ
3D structure
PDB3rr3 (R)-Profens are substrate-selective inhibitors of endocannabinoid oxygenation by COX-2.
ChainA
Resolution2.842 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Q203 H207 L384 Y385 H388 G526 S530
Catalytic site (residue number reindexed from 1) Q172 H176 L353 Y354 H357 G495 S499
Enzyme Commision number 1.14.99.1: prostaglandin-endoperoxide synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A A199 Q203 H207 F210 T212 N382 Y385 H386 H388 L391 V447 A168 Q172 H176 F179 T181 N351 Y354 H355 H357 L360 V416
BS02 FLR A R120 V349 L352 Y355 L359 Y385 W387 G526 A527 S530 R89 V318 L321 Y324 L328 Y354 W356 G495 A496 S499 BindingDB: IC50=1300nM
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0004666 prostaglandin-endoperoxide synthase activity
GO:0005515 protein binding
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0019899 enzyme binding
GO:0020037 heme binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0001516 prostaglandin biosynthetic process
GO:0001525 angiogenesis
GO:0006979 response to oxidative stress
GO:0007566 embryo implantation
GO:0007612 learning
GO:0007613 memory
GO:0008217 regulation of blood pressure
GO:0008284 positive regulation of cell population proliferation
GO:0008285 negative regulation of cell population proliferation
GO:0009410 response to xenobiotic stimulus
GO:0009624 response to nematode
GO:0009750 response to fructose
GO:0010042 response to manganese ion
GO:0010269 response to selenium ion
GO:0010575 positive regulation of vascular endothelial growth factor production
GO:0019371 cyclooxygenase pathway
GO:0030216 keratinocyte differentiation
GO:0030282 bone mineralization
GO:0031394 positive regulation of prostaglandin biosynthetic process
GO:0031622 positive regulation of fever generation
GO:0031915 positive regulation of synaptic plasticity
GO:0032227 negative regulation of synaptic transmission, dopaminergic
GO:0032310 prostaglandin secretion
GO:0032355 response to estradiol
GO:0032496 response to lipopolysaccharide
GO:0033138 positive regulation of peptidyl-serine phosphorylation
GO:0033280 response to vitamin D
GO:0034097 response to cytokine
GO:0034605 cellular response to heat
GO:0034612 response to tumor necrosis factor
GO:0035633 maintenance of blood-brain barrier
GO:0042127 regulation of cell population proliferation
GO:0042307 positive regulation of protein import into nucleus
GO:0042633 hair cycle
GO:0043065 positive regulation of apoptotic process
GO:0043066 negative regulation of apoptotic process
GO:0043154 negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
GO:0045429 positive regulation of nitric oxide biosynthetic process
GO:0045786 negative regulation of cell cycle
GO:0045907 positive regulation of vasoconstriction
GO:0045986 negative regulation of smooth muscle contraction
GO:0045987 positive regulation of smooth muscle contraction
GO:0046697 decidualization
GO:0048661 positive regulation of smooth muscle cell proliferation
GO:0050873 brown fat cell differentiation
GO:0051384 response to glucocorticoid
GO:0051926 negative regulation of calcium ion transport
GO:0051968 positive regulation of synaptic transmission, glutamatergic
GO:0070542 response to fatty acid
GO:0071222 cellular response to lipopolysaccharide
GO:0071260 cellular response to mechanical stimulus
GO:0071284 cellular response to lead ion
GO:0071318 cellular response to ATP
GO:0071456 cellular response to hypoxia
GO:0071471 cellular response to non-ionic osmotic stress
GO:0071498 cellular response to fluid shear stress
GO:0071636 positive regulation of transforming growth factor beta production
GO:0090050 positive regulation of cell migration involved in sprouting angiogenesis
GO:0090271 positive regulation of fibroblast growth factor production
GO:0090336 positive regulation of brown fat cell differentiation
GO:0090362 positive regulation of platelet-derived growth factor production
GO:0098869 cellular oxidant detoxification
GO:0150077 regulation of neuroinflammatory response
GO:1902219 negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress
GO:1905375 cellular response to homocysteine
GO:1990776 response to angiotensin
Cellular Component
GO:0005634 nucleus
GO:0005637 nuclear inner membrane
GO:0005640 nuclear outer membrane
GO:0005737 cytoplasm
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005901 caveola
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0043005 neuron projection

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3rr3, PDBe:3rr3, PDBj:3rr3
PDBsum3rr3
PubMed22053353
UniProtQ05769|PGH2_MOUSE Prostaglandin G/H synthase 2 (Gene Name=Ptgs2)

[Back to BioLiP]