6COX

CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A SELECTIVE INHIBITOR, SC-558 IN I222 SPACE GROUP

> Summary

Summary for 6COX

DescriptorCYCLOOXYGENASE-2, PROTOPORPHYRIN IX CONTAINING FE, 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
Functional Keywordsperoxidase, dioxygenase, cyclooxygenase, nonsteroidal antiinflammatory drugs, inflammation, arthritis, prostaglandin, prostaglandin synthase, oxidoreductase
Biological sourceMus musculus (house mouse)
Cellular locationMicrosome membrane; Peripheral membrane protein Q05769
Total number of polymer chains2
Total molecular weight138091.49
Authors
Kurumbail, R.,Stallings, W. (deposition date: 1996-12-18, release date: 1997-12-24, modification date: 2011-07-13)
Primary citation
Kurumbail, R.G.,Stevens, A.M.,Gierse, J.K.,McDonald, J.J.,Stegeman, R.A.,Pak, J.Y.,Gildehaus, D.,Miyashiro, J.M.,Penning, T.D.,Seibert, K.,Isakson, P.C.,Stallings, W.C.
Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents.
Nature, 384:644-648, 1996
PubMed: 8967954
DOI: 10.1038/384644a0
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers345.8%10.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 6cox
no rotation
Molmil generated image of 6cox
rotated about x axis by 90°
Molmil generated image of 6cox
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
A, BCYCLOOXYGENASE-2polymer58767319.42
UniProt (Q05769)
Pfam (PF00008)
Pfam (PF03098)
Mus musculus (house mouse)@PDBjPROSTAGLANDIN SYNTHASE-2
SUGAR (N-ACETYL-D-GLUCOSAMINE)non-polymer221.26
PROTOPORPHYRIN IX CONTAINING FEnon-polymer616.52
1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLEnon-polymer446.22

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains2
Total molecular weight134638.8
Non-Polymers*Number of molecules10
Total molecular weight3452.7
All*Total molecular weight138091.5
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.8 Å)

Cell axes181.170132.810122.740
Cell angles90.0090.0090.00
SpacegroupI 2 2 2
Resolution limits8.00 - 2.80
the highest resolution shell value2.920 - 2.800
R-factor0.22
R-work0.22000 (0.00000*)
the highest resolution shell value0.277
R-free0.30900
the highest resolution shell value0.346
RMSD bond length0.014
RMSD bond angle1.830 (1.670*)

Data Collection Statistics

Resolution limits40.00 - 2.80
the highest resolution shell value -
Number of reflections35324
Number of measurements818993*
Rmerge_l_obs0.088
the highest resolution shell value0.326
Completeness96.9
the highest resolution shell value92.7*
Redundancy4.35
the highest resolution shell value3.1
I/sigma(I)-0.5

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1Vapor diffusion, hanging drop*818**

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropinhibitor0.6 (%)
21reservoirmPEG55020-34 (%)
31reservoir240 (mM)
41reservoirEPPS50 (mM)
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005901cellular_componentcaveola
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0043005cellular_componentneuron projection
A0043234cellular_componentprotein complex
A0019899molecular_functionenzyme binding
A0020037molecular_functionheme binding
A0008289molecular_functionlipid binding
A0046872molecular_functionmetal ion binding
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0004601molecular_functionperoxidase activity
A0004666molecular_functionprostaglandin-endoperoxide synthase activity
A0042803molecular_functionprotein homodimerization activity
A0001525biological_processangiogenesis
A0030282biological_processbone mineralization
A0050873biological_processbrown fat cell differentiation
A0071318biological_processcellular response to ATP
A0071498biological_processcellular response to fluid shear stress
A0071456biological_processcellular response to hypoxia
A0071260biological_processcellular response to mechanical stimulus
A0034644biological_processcellular response to UV
A0019371biological_processcyclooxygenase pathway
A0046697biological_processdecidualization
A0007566biological_processembryo implantation
A0042633biological_processhair cycle
A0006954biological_processinflammatory response
A0030216biological_processkeratinocyte differentiation
A0007612biological_processlearning
A0035633biological_processmaintenance of blood-brain barrier
A0007613biological_processmemory
A0051926biological_processnegative regulation of calcium ion transport
A0045786biological_processnegative regulation of cell cycle
A0008285biological_processnegative regulation of cell proliferation
A0045986biological_processnegative regulation of smooth muscle contraction
A0032227biological_processnegative regulation of synaptic transmission, dopaminergic
A0030728biological_processovulation
A0043065biological_processpositive regulation of apoptotic process
A0090336biological_processpositive regulation of brown fat cell differentiation
A0090050biological_processpositive regulation of cell migration involved in sprouting angiogenesis
A0031622biological_processpositive regulation of fever generation
A0090271biological_processpositive regulation of fibroblast growth factor production
A0042346biological_processpositive regulation of NF-kappaB import into nucleus
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0090362biological_processpositive regulation of platelet-derived growth factor production
A0048661biological_processpositive regulation of smooth muscle cell proliferation
A0045987biological_processpositive regulation of smooth muscle contraction
A0031915biological_processpositive regulation of synaptic plasticity
A0051968biological_processpositive regulation of synaptic transmission, glutamatergic
A0071636biological_processpositive regulation of transforming growth factor beta production
A0010575biological_processpositive regulation of vascular endothelial growth factor production
A0045907biological_processpositive regulation of vasoconstriction
A0001516biological_processprostaglandin biosynthetic process
A0008217biological_processregulation of blood pressure
A0042127biological_processregulation of cell proliferation
A0042493biological_processresponse to drug
A0032355biological_processresponse to estradiol
A0070542biological_processresponse to fatty acid
A0009750biological_processresponse to fructose
A0051384biological_processresponse to glucocorticoid
A0032496biological_processresponse to lipopolysaccharide
A0010226biological_processresponse to lithium ion
A0010042biological_processresponse to manganese ion
A0006979biological_processresponse to oxidative stress
A0034612biological_processresponse to tumor necrosis factor
A0033280biological_processresponse to vitamin D
A0019233biological_processsensory perception of pain
B0005901cellular_componentcaveola
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0043005cellular_componentneuron projection
B0043234cellular_componentprotein complex
B0019899molecular_functionenzyme binding
B0020037molecular_functionheme binding
B0008289molecular_functionlipid binding
B0046872molecular_functionmetal ion binding
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0004601molecular_functionperoxidase activity
B0004666molecular_functionprostaglandin-endoperoxide synthase activity
B0042803molecular_functionprotein homodimerization activity
B0001525biological_processangiogenesis
B0030282biological_processbone mineralization
B0050873biological_processbrown fat cell differentiation
B0071318biological_processcellular response to ATP
B0071498biological_processcellular response to fluid shear stress
B0071456biological_processcellular response to hypoxia
B0071260biological_processcellular response to mechanical stimulus
B0034644biological_processcellular response to UV
B0019371biological_processcyclooxygenase pathway
B0046697biological_processdecidualization
B0007566biological_processembryo implantation
B0042633biological_processhair cycle
B0006954biological_processinflammatory response
B0030216biological_processkeratinocyte differentiation
B0007612biological_processlearning
B0035633biological_processmaintenance of blood-brain barrier
B0007613biological_processmemory
B0051926biological_processnegative regulation of calcium ion transport
B0045786biological_processnegative regulation of cell cycle
B0008285biological_processnegative regulation of cell proliferation
B0045986biological_processnegative regulation of smooth muscle contraction
B0032227biological_processnegative regulation of synaptic transmission, dopaminergic
B0030728biological_processovulation
B0043065biological_processpositive regulation of apoptotic process
B0090336biological_processpositive regulation of brown fat cell differentiation
B0090050biological_processpositive regulation of cell migration involved in sprouting angiogenesis
B0031622biological_processpositive regulation of fever generation
B0090271biological_processpositive regulation of fibroblast growth factor production
B0042346biological_processpositive regulation of NF-kappaB import into nucleus
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0090362biological_processpositive regulation of platelet-derived growth factor production
B0048661biological_processpositive regulation of smooth muscle cell proliferation
B0045987biological_processpositive regulation of smooth muscle contraction
B0031915biological_processpositive regulation of synaptic plasticity
B0051968biological_processpositive regulation of synaptic transmission, glutamatergic
B0071636biological_processpositive regulation of transforming growth factor beta production
B0010575biological_processpositive regulation of vascular endothelial growth factor production
B0045907biological_processpositive regulation of vasoconstriction
B0001516biological_processprostaglandin biosynthetic process
B0008217biological_processregulation of blood pressure
B0042127biological_processregulation of cell proliferation
B0042493biological_processresponse to drug
B0032355biological_processresponse to estradiol
B0070542biological_processresponse to fatty acid
B0009750biological_processresponse to fructose
B0051384biological_processresponse to glucocorticoid
B0032496biological_processresponse to lipopolysaccharide
B0010226biological_processresponse to lithium ion
B0010042biological_processresponse to manganese ion
B0006979biological_processresponse to oxidative stress
B0034612biological_processresponse to tumor necrosis factor
B0033280biological_processresponse to vitamin D
B0019233biological_processsensory perception of pain
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
CAT1TYR 385 IS BELIEVED TO BE THE AMINO ACID THAT ABSTRACTS A HYDROGEN ATOM FROM THE SUBSTRATE. IT IS LOCATED CLOSE TO THE HEME. A TYROSINE RADICAL IS FORMED DURING THE COURSE OF THE REACTION.
ChainResidue
ATYR354

ACE1SER 530 IS ACETYLATED BY ASPIRIN (AN ACETYL GROUP IS COVALENTLY ATTACHED TO THE PROTEIN WHEN INHIBITED WITH ASPIRIN). THE ACETYLATED SER PREVENTS THE PROPER BINDING OF THE SUBSTRATE IN THE CYCLOOXYGENASE ACTIVE SITE. IT HAS BEEN RECENTLY SHOWN, HOWEVER, THAT ACETYLATION OF CYCLOOXYGENASE-2 RESULTS IN THE FORMATION OF A DIFFERENT PRODUCT (15-HETE).
ChainResidue
ASER499

HEM1HIS 388 IS THE AXIAL LIGAND TO THE HEME.
ChainResidue
AHIS357

SUB1ARGININE 120 IS BELIEVED TO ANCHOR THE CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.
ChainResidue
AARG89

AC14BINDING SITE FOR RESIDUE NAG A 661
ChainResidue
APRO8
ATYR23
AGLU35
AASN36

AC23BINDING SITE FOR RESIDUE NAG A 671
ChainResidue
AASN113
ATYR116
AARG185

AC34BINDING SITE FOR RESIDUE NAG A 681
ChainResidue
ATYR371
AASN379
ASER381
AILE382

AC44BINDING SITE FOR RESIDUE NAG B 661
ChainResidue
BPRO8
BTYR23
BGLU35
BASN36

AC54BINDING SITE FOR RESIDUE NAG B 671
ChainResidue
BGLU109
BASN113
BTYR116
BARG185

AC64BINDING SITE FOR RESIDUE NAG B 681
ChainResidue
BTYR371
BASN379
BSER381
BILE382

AC715BINDING SITE FOR RESIDUE HEM A 682
ChainResidue
AALA168
AGLN172
AHIS176
APHE179
ALYS180
ATHR181
AHIS183
AVAL264
AASN351
ATYR354
AHIS355
AHIS357
ALEU360
AVAL416
AGLN423

AC816BINDING SITE FOR RESIDUE S58 A 701
ChainResidue
AHIS58
AARG89
AGLN161
AVAL318
ALEU321
ASER322
ATYR324
ALEU328
ATYR354
ATRP356
AALA485
APHE487
AVAL492
AGLY495
AALA496
ALEU500

AC914BINDING SITE FOR RESIDUE HEM B 682
ChainResidue
BALA168
BGLN172
BHIS176
BPHE179
BLYS180
BTHR181
BHIS183
BVAL264
BASN351
BTYR354
BHIS355
BHIS357
BVAL416
BGLN423

BC117BINDING SITE FOR RESIDUE S58 B 701
ChainResidue
BHIS58
BARG89
BGLN161
BVAL318
BLEU321
BSER322
BTYR324
BLEU328
BTYR354
BTRP356
BARG482
BALA485
BPHE487
BVAL492
BGLY495
BALA496
BLEU500

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
NAG_6cox_A_6616N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
ASER38NAG: N-ACETYL-D-GLUCOSAMINE
APRO40NAG: N-ACETYL-D-GLUCOSAMINE
ATYR55NAG: N-ACETYL-D-GLUCOSAMINE
AGLU67-ASN68NAG: N-ACETYL-D-GLUCOSAMINE
ATHR70NAG: N-ACETYL-D-GLUCOSAMINE

S58_6cox_A_701241-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE binding site
ChainResidueligand
AHIS90S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AVAL116S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AARG120S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AGLN192S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AVAL349S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
ALEU352-TYR355S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
ALEU359S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
APHE381S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
ALEU384-TYR385S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
ATRP387S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AARG513S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AALA516-PHE518S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AMET522-VAL523S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
AGLY526-ALA527S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
ASER530-LEU531S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE

NAG_6cox_A_6718N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
AHIS133NAG: N-ACETYL-D-GLUCOSAMINE
AGLU140NAG: N-ACETYL-D-GLUCOSAMINE
AASN144NAG: N-ACETYL-D-GLUCOSAMINE
ASER146-TYR147NAG: N-ACETYL-D-GLUCOSAMINE
AARG216NAG: N-ACETYL-D-GLUCOSAMINE
APHE220NAG: N-ACETYL-D-GLUCOSAMINE
BLEU238NAG: N-ACETYL-D-GLUCOSAMINE

HEM_6cox_A_68226PROTOPORPHYRIN IX CONTAINING FE binding site
ChainResidueligand
ATYR148HEM: PROTOPORPHYRIN IX CONTAINING FE
AALA199-PHE200HEM: PROTOPORPHYRIN IX CONTAINING FE
AALA202-GLN203HEM: PROTOPORPHYRIN IX CONTAINING FE
ATHR206-HIS207HEM: PROTOPORPHYRIN IX CONTAINING FE
APHE210-THR212HEM: PROTOPORPHYRIN IX CONTAINING FE
AHIS214HEM: PROTOPORPHYRIN IX CONTAINING FE
AVAL295HEM: PROTOPORPHYRIN IX CONTAINING FE
AASN382HEM: PROTOPORPHYRIN IX CONTAINING FE
ATYR385-HIS388HEM: PROTOPORPHYRIN IX CONTAINING FE
ALEU390-LEU391HEM: PROTOPORPHYRIN IX CONTAINING FE
APHE404HEM: PROTOPORPHYRIN IX CONTAINING FE
ALEU408HEM: PROTOPORPHYRIN IX CONTAINING FE
AVAL444HEM: PROTOPORPHYRIN IX CONTAINING FE
AVAL447HEM: PROTOPORPHYRIN IX CONTAINING FE
AALA450-SER451HEM: PROTOPORPHYRIN IX CONTAINING FE
AGLN454HEM: PROTOPORPHYRIN IX CONTAINING FE

NAG_6cox_B_6718N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
ALEU238NAG: N-ACETYL-D-GLUCOSAMINE
BHIS133NAG: N-ACETYL-D-GLUCOSAMINE
BGLU140NAG: N-ACETYL-D-GLUCOSAMINE
BASN144NAG: N-ACETYL-D-GLUCOSAMINE
BSER146-TYR147NAG: N-ACETYL-D-GLUCOSAMINE
BARG216NAG: N-ACETYL-D-GLUCOSAMINE
BPHE220NAG: N-ACETYL-D-GLUCOSAMINE

NAG_6cox_A_6818N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
ATYR402NAG: N-ACETYL-D-GLUCOSAMINE
ALYS405-GLN406NAG: N-ACETYL-D-GLUCOSAMINE
AASN410NAG: N-ACETYL-D-GLUCOSAMINE
ASER412-ILE413NAG: N-ACETYL-D-GLUCOSAMINE
AGLU416-HIS417NAG: N-ACETYL-D-GLUCOSAMINE

NAG_6cox_B_6616N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
BSER38NAG: N-ACETYL-D-GLUCOSAMINE
BPRO40NAG: N-ACETYL-D-GLUCOSAMINE
BTYR55NAG: N-ACETYL-D-GLUCOSAMINE
BGLU67-ASN68NAG: N-ACETYL-D-GLUCOSAMINE
BTHR70NAG: N-ACETYL-D-GLUCOSAMINE

S58_6cox_B_701241-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE binding site
ChainResidueligand
BHIS90S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BVAL116S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BARG120S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BGLN192S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BVAL349S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BLEU352-TYR355S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BLEU359S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BPHE381S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BLEU384-TYR385S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BTRP387S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BARG513S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BALA516-PHE518S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BMET522-VAL523S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BGLY526-ALA527S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE
BSER530-LEU531S58: 1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE

HEM_6cox_B_68226PROTOPORPHYRIN IX CONTAINING FE binding site
ChainResidueligand
BTYR148HEM: PROTOPORPHYRIN IX CONTAINING FE
BALA199-PHE200HEM: PROTOPORPHYRIN IX CONTAINING FE
BALA202-GLN203HEM: PROTOPORPHYRIN IX CONTAINING FE
BTHR206-HIS207HEM: PROTOPORPHYRIN IX CONTAINING FE
BPHE210-THR212HEM: PROTOPORPHYRIN IX CONTAINING FE
BHIS214HEM: PROTOPORPHYRIN IX CONTAINING FE
BVAL295HEM: PROTOPORPHYRIN IX CONTAINING FE
BASN382HEM: PROTOPORPHYRIN IX CONTAINING FE
BTYR385-HIS388HEM: PROTOPORPHYRIN IX CONTAINING FE
BLEU390-LEU391HEM: PROTOPORPHYRIN IX CONTAINING FE
BPHE404HEM: PROTOPORPHYRIN IX CONTAINING FE
BLEU408HEM: PROTOPORPHYRIN IX CONTAINING FE
BVAL444HEM: PROTOPORPHYRIN IX CONTAINING FE
BVAL447HEM: PROTOPORPHYRIN IX CONTAINING FE
BALA450-SER451HEM: PROTOPORPHYRIN IX CONTAINING FE
BGLN454HEM: PROTOPORPHYRIN IX CONTAINING FE

NAG_6cox_B_6817N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
BTYR402NAG: N-ACETYL-D-GLUCOSAMINE
BGLN406NAG: N-ACETYL-D-GLUCOSAMINE
BASN410NAG: N-ACETYL-D-GLUCOSAMINE
BSER412-ILE413NAG: N-ACETYL-D-GLUCOSAMINE
BGLU416-HIS417NAG: N-ACETYL-D-GLUCOSAMINE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI11For cyclooxygenase activity.
ChainResidueDetails
ATYR354

SWS_FT_FI21Proton acceptor.
ChainResidueDetails
AHIS176

SWS_FT_FI61For cyclooxygenase activity.
ChainResidueDetails
BTYR354

SWS_FT_FI71Proton acceptor.
ChainResidueDetails
BHIS176

?

Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA11Annotated By Reference To The Literature 1mhl
ChainResidueDetails
AVAL291

CSA21Annotated By Reference To The Literature 1mhl
ChainResidueDetails
BVAL291

CSA33Annotated By Reference To The Literature 1mhl
ChainResidueDetails
AHIS207
ATYR385
AGLN203

CSA43Annotated By Reference To The Literature 1mhl
ChainResidueDetails
BHIS207
BTYR385
BGLN203

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Catalytic Information from CATRES

site_idNumber of ResiduesDetails
extCATRES13Mapped from 5cox to 6cox using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 20269363, 20290850, 20463516, 91056037, 91177862, 97407953
ChainResidueDetails
AGLN203activates substrate. assist in peroxide formation
AHIS207activates substrate. assist in peroxide formation
ATYR385radical. Radical

> Sequence Neighbor

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