Structure of PDB 5kir Chain B Binding Site BS02

Receptor Information
>5kir Chain B (length=551) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFLTRIKLFLK
PTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNA
DYGYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLL
LRRKFIPDPQGSNMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNH
IYGETLARQRKLRLFKDGKMKYQIIDGEMYPPTVKDTQAEMIYPPQVPEH
LRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTS
RLILIGETIKIVIEDYVNHLSGYHFKLKFDPELLFNKQFQYQNRIAAEFN
TLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAG
RVAGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELT
GEKEMSAELEALYGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLK
GLMGNVICSPAYWKPSTFGGEVGFQIINTASIQSLICNNVKGCPFTSFSV
P
Ligand information
Ligand IDCOH
InChIInChI=1S/C34H34N4O4.Co/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyAQTFKGDWFRRIHR-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Co]36[N]7=C(C=C8N6C(=C5)C(=C8C=C)C)C(=C(C7=C2)C=C)C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Co][N@@]5C(=CC1=N2)C(=C(C=C)C5=CC6=NC(=Cc4c(C)c3CCC(O)=O)C(=C6C)C=C)C
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Co][N]5C(=CC1=N2)C(=C(C=C)C5=CC6=NC(=Cc4c(C)c3CCC(O)=O)C(=C6C)C=C)C
FormulaC34 H32 Co N4 O4
NamePROTOPORPHYRIN IX CONTAINING CO
ChEMBL
DrugBank
ZINC
PDB chain5kir Chain B Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB5kir Crystal structure of rofecoxib bound to human cyclooxygenase-2.
Resolution2.697 Å
Binding residue
(original residue number in PDB)		Q203 F210 K211 T212 H214 N382 Y385 H386 H388 L391 V447
Binding residue
(residue number reindexed from 1)		Q171 F178 K179 T180 H182 N350 Y353 H354 H356 L359 V415
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q203 H207 L384 Y385 H388 G526 S530
Catalytic site (residue number reindexed from 1) Q171 H175 L352 Y353 H356 G494 S498
Enzyme Commision number 1.14.99.1: prostaglandin-endoperoxide synthase.
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5kir, PDBe:5kir, PDBj:5kir
PDBsum5kir
PubMed27710942
UniProtP35354|PGH2_HUMAN Prostaglandin G/H synthase 2 (Gene Name=PTGS2)

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