Structure of PDB 5ikq Chain B
Receptor sequence
>5ikqB (length=551) Species:
9606
(Homo sapiens) [
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NPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLK
PTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNA
DYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLL
LRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNH
IYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEH
LRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTS
RLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFN
TLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAG
RVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELT
GEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLK
GLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKGCPFTSFSV
P
3D structure
PDB
5ikq
Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid Derivatives Is Dependent on Peroxide Tone.
Chain
B
Resolution
2.41 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB)
Q204 H208 L385 Y386 H389 G527 S531
Catalytic site (residue number reindexed from 1)
Q171 H175 L352 Y353 H356 G494 S498
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
COH
B
Q204 H208 F211 K212 T213 N383 Y386 H387 W388 H389 L392 V448
Q171 H175 F178 K179 T180 N350 Y353 H354 W355 H356 L359 V415
BS02
JMS
B
V350 L353 Y386 G527 A528 S531 L532
V317 L320 Y353 G494 A495 S498 L499
BindingDB: Ki=700nM,IC50=50nM
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: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:0050727
regulation of inflammatory response
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:0005788
endoplasmic reticulum lumen
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:5ikq
,
PDBe:5ikq
,
PDBj:5ikq
PDBsum
5ikq
PubMed
27226593
UniProt
P35354
|PGH2_HUMAN Prostaglandin G/H synthase 2 (Gene Name=PTGS2)
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