Structure of PDB 4z0l Chain C
Receptor sequence
>4z0lC (length=551) Species:
10090
(Mus musculus) [
Search protein sequence
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ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLL
KPTPNTVHYILTHFKGVWNIVNNIPFLRSLIMKYVLTSRSYLIDSPPTYN
VHYGYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGNKELPDSKEVLEKV
LLRREFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQVEMIYPPHIPE
NLQFAVGQEVFGLVPGLMMYATIWLREHNRVCDILKQEHPEWGDEQLFQT
SRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIASEF
NTLYHWHPLLPDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFSLKPYTSFEEL
TGEKEMAAELKALYSDIDVMELYPALLVEKPRPDAIFGETMVELGAPFSL
KGLMGNPICSPQYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTSFN
V
3D structure
PDB
4z0l
nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2.
Chain
C
Resolution
2.29 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
C
A202 Q203 H207 F210 T212 H214 N382 Y385 H386 H388 L391 V447
A171 Q172 H176 F179 T181 H183 N351 Y354 H355 H357 L360 V416
BS02
4LA
C
H90 M113 V116 L117 R120 V349 S353 Y355 W387 V523 A527 L531
H58 M82 V85 L86 R89 V318 S322 Y324 W356 V492 A496 L500
MOAD
: ic50=0.051uM
BS03
N1B
C
H90 M113 V116 L117 R120 V349 S353 Y355 L359 W387 V523 A527 L531
H58 M82 V85 L86 R89 V318 S322 Y324 L328 W356 V492 A496 L500
MOAD
: ic50=0.051uM
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:4z0l
,
PDBe:4z0l
,
PDBj:4z0l
PDBsum
4z0l
PubMed
26088701
UniProt
Q05769
|PGH2_MOUSE Prostaglandin G/H synthase 2 (Gene Name=Ptgs2)
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