Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T66665 | Target Info | |||
| Target Name | Prostaglandin G/H synthase 2 (COX-2) | ||||
| Synonyms | Prostaglandin-endoperoxide synthase 2; Prostaglandin H2 synthase 2; PHS II; PGHS-2; PGH synthase 2; Cyclooxygenase-2; COX2; COX-2 | ||||
| Target Type | Successful Target | ||||
| Gene Name | PTGS2 | ||||
| Biochemical Class | Paired donor oxygen oxidoreductase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | PROTOPORPHYRIN IX CONTAINING CO | Ligand Info | |||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 5F1A The Crystal Structure of Salicylate Bound to Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.38 Å | Mutation | No | [1] |
| PDB Sequence |
KNPCCSHPCQ
42 NRGVCMSVGF52 DQYKCDCTRT62 GFYGENCSTP72 EFLTRIKLFL82 KPTPNTVHYI 92 LTHFKGFWNV102 VNNIPFLRNA111 IMSYVLTSRS121 HLIDSPPTYN131 ADYGYKSWEA 141 FSNLSYYTRA151 LPPVPDDCPT161 PLGVKGKKQL171 PDSNEIVEKL181 LLRRKFIPDP 191 QGSNMMFAFF201 AQHFTHQFFK211 TDHKRGPAFT221 NGLGHGVDLN231 HIYGETLARQ 241 RKLRLFKDGK251 MKYQIIDGEM261 YPPTVKDTQA271 EMIYPPQVPE281 HLRFAVGQEV 291 FGLVPGLMMY301 ATIWLREHNR311 VCDVLKQEHP321 EWGDEQLFQT331 SRLILIGETI 341 KIVIEDYVQH351 LSGYHFKLKF361 DPELLFNKQF371 QYQNRIAAEF381 NTLYHWHPLL 391 PDTFQIHDQK401 YNYQQFIYNN411 SILLEHGITQ421 FVESFTRQIA431 GRVAGGRNVP 441 PAVQKVSQAS451 IDQSRQMKYQ461 SFNEYRKRFM471 LKPYESFEEL481 TGEKEMSAEL 491 EALYGDIDAV501 ELYPALLVEK511 PRPDAIFGET521 MVEVGAPFSL531 KGLMGNVICS 541 PAYWKPSTFG551 GEVGFQIINT561 ASIQSLICNN571 VKGCPFTSFS581 VPD |
|||||
|
|
TYR148
3.462
ALA199
3.420
PHE200
4.742
ALA202
3.345
GLN203
3.313
THR206
4.747
HIS207
3.788
PHE210
3.339
LYS211
3.922
THR212
1.283
HIS214
3.329
LEU294
3.996
VAL295
3.776
ASN382
2.920
|
|||||
| PDB ID: 5F19 The Crystal Structure of Aspirin Acetylated Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.04 Å | Mutation | No | [1] |
| PDB Sequence |
KNPCCSHPCQ
42 NRGVCMSVGF52 DQYKCDCTRT62 GFYGENCSTP72 EFLTRIKLFL82 KPTPNTVHYI 92 LTHFKGFWNV102 VNNIPFLRNA111 IMSYVLTSRS121 HLIDSPPTYN131 ADYGYKSWEA 141 FSNLSYYTRA151 LPPVPDDCPT161 PLGVKGKKQL171 PDSNEIVEKL181 LLRRKFIPDP 191 QGSNMMFAFF201 AQHFTHQFFK211 TDHKRGPAFT221 NGLGHGVDLN231 HIYGETLARQ 241 RKLRLFKDGK251 MKYQIIDGEM261 YPPTVKDTQA271 EMIYPPQVPE281 HLRFAVGQEV 291 FGLVPGLMMY301 ATIWLREHNR311 VCDVLKQEHP321 EWGDEQLFQT331 SRLILIGETI 341 KIVIEDYVQH351 LSGYHFKLKF361 DPELLFNKQF371 QYQNRIAAEF381 NTLYHWHPLL 391 PDTFQIHDQK401 YNYQQFIYNN411 SILLEHGITQ421 FVESFTRQIA431 GRVAGGRNVP 441 PAVQKVSQAS451 IDQSRQMKYQ461 SFNEYRKRFM471 LKPYESFEEL481 TGEKEMSAEL 491 EALYGDIDAV501 ELYPALLVEK511 PRPDAIFGET521 MVEVGAPFLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
|
TYR148
3.687
ALA199
3.295
PHE200
3.608
ALA202
3.438
GLN203
3.386
THR206
4.969
HIS207
3.664
PHE210
3.465
LYS211
3.843
THR212
1.642
HIS214
2.878
LEU294
4.612
VAL295
3.913
ASN382
3.095
|
|||||
| PDB ID: 5IKR The Structure of Mefenamic Acid Bound to Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.34 Å | Mutation | No | [2] |
| PDB Sequence |
NPCCSHPCQN
43 RGVCMSVGFD53 QYKCDCTRTG63 FYGENCSTPE73 FLTRIKLFLK83 PTPNTVHYIL 93 THFKGFWNVV103 NNIPFLRNAI112 MSYVLTSRSH122 LIDSPPTYNA132 DYGYKSWEAF 142 SNLSYYTRAL152 PPVPDDCPTP162 LGVKGKKQLP172 DSNEIVEKLL182 LRRKFIPDPQ 192 GSNMMFAFFA202 QHFTHQFFKT212 DHKRGPAFTN222 GLGHGVDLNH232 IYGETLARQR 242 KLRLFKDGKM252 KYQIIDGEMY262 PPTVKDTQAE272 MIYPPQVPEH282 LRFAVGQEVF 292 GLVPGLMMYA302 TIWLREHNRV312 CDVLKQEHPE322 WGDEQLFQTS332 RLILIGETIK 342 IVIEDYVQHL352 SGYHFKLKFD362 PELLFNKQFQ372 YQNRIAAEFN382 TLYHWHPLLP 392 DTFQIHDQKY402 NYQQFIYNNS412 ILLEHGITQF422 VESFTRQIAG432 RVAGGRNVPP 442 AVQKVSQASI452 DQSRQMKYQS462 FNEYRKRFML472 KPYESFEELT482 GEKEMSAELE 492 ALYGDIDAVE502 LYPALLVEKP512 RPDAIFGETM522 VEVGAPFSLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
|
TYR148
3.354
MET196
4.842
ALA199
2.772
PHE200
2.302
ALA202
2.255
GLN203
2.263
THR206
3.773
HIS207
2.671
PHE210
2.221
LYS211
3.105
THR212
1.282
HIS214
2.979
LEU294
2.880
VAL295
2.661
TYR348
4.749
|
|||||
| PDB ID: 5IKQ The Structure of Meclofenamic Acid Bound to Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.41 Å | Mutation | No | [2] |
| PDB Sequence |
NPCCSHPCQN
43 RGVCMSVGFD53 QYKCDCTRTG63 FYGENCSTPE73 FLTRIKLFLK83 PTPNTVHYIL 93 THFKGFWNVV103 NNIPFLRNAI112 MSYVLTSRSH122 LIDSPPTYNA132 DYGYKSWEAF 142 SNLSYYTRAL152 PPVPDDCPTP162 LGVKGKKQLP172 DSNEIVEKLL182 LRRKFIPDPQ 192 GSNMMFAFFA202 QHFTHQFFKT212 DHKRGPAFTN222 GLGHGVDLNH232 IYGETLARQR 242 KLRLFKDGKM252 KYQIIDGEMY262 PPTVKDTQAE272 MIYPPQVPEH282 LRFAVGQEVF 292 GLVPGLMMYA302 TIWLREHNRV312 CDVLKQEHPE322 WGDEQLFQTS332 RLILIGETIK 342 IVIEDYVQHL352 SGYHFKLKFD362 PELLFNKQFQ372 YQNRIAAEFN382 TLYHWHPLLP 392 DTFQIHDQKY402 NYQQFIYNNS412 ILLEHGITQF422 VESFTRQIAG432 RVAGGRNVPP 442 AVQKVSQASI452 DQSRQMKYQS462 FNEYRKRFML472 KPYESFEELT482 GEKEMSAELE 492 ALYGDIDAVE502 LYPALLVEKP512 RPDAIFGETM522 VEVGAPFSLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .COH or .COH2 or .COH3 or :3COH;style chemicals stick;color identity;select .A:148 or .A:199 or .A:200 or .A:202 or .A:203 or .A:206 or .A:207 or .A:210 or .A:211 or .A:212 or .A:214 or .A:294 or .A:295 or .A:348 or .A:382 or .A:385 or .A:386 or .A:387 or .A:388 or .A:390 or .A:391 or .A:395 or .A:404 or .A:407 or .A:408 or .A:444 or .A:447 or .A:450 or .A:454; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TYR148
3.153
ALA199
3.073
PHE200
3.415
ALA202
2.646
GLN203
2.424
THR206
4.011
HIS207
2.889
PHE210
2.099
LYS211
3.021
THR212
1.278
HIS214
3.092
LEU294
2.500
VAL295
2.886
TYR348
4.966
ASN382
2.728
|
|||||
| PDB ID: 5IKT The Structure of Tolfenamic Acid Bound to Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.45 Å | Mutation | No | [2] |
| PDB Sequence |
NPCCSHPCQN
43 RGVCMSVGFD53 QYKCDCTRTG63 FYGENCSTPE73 FLTRIKLFLK83 PTPNTVHYIL 93 THFKGFWNVV103 NNIPFLRNAI112 MSYVLTSRSH122 LIDSPPTYNA132 DYGYKSWEAF 142 SNLSYYTRAL152 PPVPDDCPTP162 LGVKGKKQLP172 DSNEIVEKLL182 LRRKFIPDPQ 192 GSNMMFAFFA202 QHFTHQFFKT212 DHKRGPAFTN222 GLGHGVDLNH232 IYGETLARQR 242 KLRLFKDGKM252 KYQIIDGEMY262 PPTVKDTQAE272 MIYPPQVPEH282 LRFAVGQEVF 292 GLVPGLMMYA302 TIWLREHNRV312 CDVLKQEHPE322 WGDEQLFQTS332 RLILIGETIK 342 IVIEDYVQHL352 SGYHFKLKFD362 PELLFNKQFQ372 YQNRIAAEFN382 TLYHWHPLLP 392 DTFQIHDQKY402 NYQQFIYNNS412 ILLEHGITQF422 VESFTRQIAG432 RVAGGRNVPP 442 AVQKVSQASI452 DQSRQMKYQS462 FNEYRKRFML472 KPYESFEELT482 GEKEMSAELE 492 ALYGDIDAVE502 LYPALLVEKP512 RPDAIFGETM522 VEVGAPFSLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .COH or .COH2 or .COH3 or :3COH;style chemicals stick;color identity;select .A:148 or .A:199 or .A:200 or .A:202 or .A:203 or .A:206 or .A:207 or .A:210 or .A:211 or .A:212 or .A:214 or .A:294 or .A:295 or .A:348 or .A:382 or .A:385 or .A:386 or .A:387 or .A:388 or .A:390 or .A:391 or .A:395 or .A:404 or .A:407 or .A:408 or .A:444 or .A:447 or .A:450 or .A:454; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TYR148
3.161
ALA199
2.859
PHE200
3.213
ALA202
2.918
GLN203
2.392
THR206
3.761
HIS207
2.645
PHE210
2.093
LYS211
3.525
THR212
1.273
HIS214
3.305
LEU294
2.558
VAL295
2.606
TYR348
4.955
ASN382
2.249
|
|||||
| PDB ID: 5IKV The Structure of Flufenamic Acid Bound to Human Cyclooxygenase-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.51 Å | Mutation | No | [2] |
| PDB Sequence |
NPCCSHPCQN
43 RGVCMSVGFD53 QYKCDCTRTG63 FYGENCSTPE73 FLTRIKLFLK83 PTPNTVHYIL 93 THFKGFWNVV103 NNIPFLRNAI112 MSYVLTSRSH122 LIDSPPTYNA132 DYGYKSWEAF 142 SNLSYYTRAL152 PPVPDDCPTP162 LGVKGKKQLP172 DSNEIVEKLL182 LRRKFIPDPQ 192 GSNMMFAFFA202 QHFTHQFFKT212 DHKRGPAFTN222 GLGHGVDLNH232 IYGETLARQR 242 KLRLFKDGKM252 KYQIIDGEMY262 PPTVKDTQAE272 MIYPPQVPEH282 LRFAVGQEVF 292 GLVPGLMMYA302 TIWLREHNRV312 CDVLKQEHPE322 WGDEQLFQTS332 RLILIGETIK 342 IVIEDYVQHL352 SGYHFKLKFD362 PELLFNKQFQ372 YQNRIAAEFN382 TLYHWHPLLP 392 DTFQIHDQKY402 NYQQFIYNNS412 ILLEHGITQF422 VESFTRQIAG432 RVAGGRNVPP 442 AVQKVSQASI452 DQSRQMKYQS462 FNEYRKRFML472 KPYESFEELT482 GEKEMSAELE 492 ALYGDIDAVE502 LYPALLVEKP512 RPDAIFGETM522 VEVGAPFSLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .COH or .COH2 or .COH3 or :3COH;style chemicals stick;color identity;select .A:148 or .A:196 or .A:199 or .A:200 or .A:202 or .A:203 or .A:206 or .A:207 or .A:210 or .A:211 or .A:212 or .A:214 or .A:294 or .A:295 or .A:348 or .A:382 or .A:385 or .A:386 or .A:387 or .A:388 or .A:390 or .A:391 or .A:395 or .A:404 or .A:407 or .A:408 or .A:444 or .A:447 or .A:450 or .A:454; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TYR148
3.553
MET196
4.917
ALA199
2.685
PHE200
2.137
ALA202
2.290
GLN203
2.332
THR206
3.764
HIS207
2.781
PHE210
2.629
LYS211
3.112
THR212
2.174
HIS214
2.905
LEU294
2.646
VAL295
2.332
TYR348
4.817
|
|||||
| PDB ID: 5KIR The Structure of Vioxx Bound to Human COX-2 | ||||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | No | [3] |
| PDB Sequence |
NPCCSHPCQN
43 RGVCMSVGFD53 QYKCDCTRTG63 FYGENCSTPE73 FLTRIKLFLK83 PTPNTVHYIL 93 THFKGFWNVV103 NNIPFLRNAI112 MSYVLTSRSH122 LIDSPPTYNA132 DYGYKSWEAF 142 SNLSYYTRAL152 PPVPDDCPTP162 LGVKGKKQLP172 DSNEIVEKLL182 LRRKFIPDPQ 192 GSNMMFAFFA202 QHFTHQFFKT212 DHKRGPAFTN222 GLGHGVDLNH232 IYGETLARQR 242 KLRLFKDGKM252 KYQIIDGEMY262 PPTVKDTQAE272 MIYPPQVPEH282 LRFAVGQEVF 292 GLVPGLMMYA302 TIWLREHNRV312 CDVLKQEHPE322 WGDEQLFQTS332 RLILIGETIK 342 IVIEDYVNHL352 SGYHFKLKFD362 PELLFNKQFQ372 YQNRIAAEFN382 TLYHWHPLLP 392 DTFQIHDQKY402 NYQQFIYNNS412 ILLEHGITQF422 VESFTRQIAG432 RVAGGRNVPP 442 AVQKVSQASI452 DQSRQMKYQS462 FNEYRKRFML472 KPYESFEELT482 GEKEMSAELE 492 ALYGDIDAVE502 LYPALLVEKP512 RPDAIFGETM522 VEVGAPFSLK532 GLMGNVICSP 542 AYWKPSTFGG552 EVGFQIINTA562 SIQSLICNNV572 KGCPFTSFSV582 P |
|||||
|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .COH or .COH2 or .COH3 or :3COH;style chemicals stick;color identity;select .A:148 or .A:196 or .A:199 or .A:200 or .A:202 or .A:203 or .A:206 or .A:207 or .A:210 or .A:211 or .A:212 or .A:214 or .A:294 or .A:295 or .A:348 or .A:382 or .A:385 or .A:386 or .A:387 or .A:388 or .A:390 or .A:391 or .A:392 or .A:395 or .A:404 or .A:407 or .A:408 or .A:444 or .A:447 or .A:450 or .A:454; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TYR148
3.814
MET196
4.482
ALA199
2.511
PHE200
2.607
ALA202
2.359
GLN203
2.252
THR206
3.853
HIS207
3.494
PHE210
2.330
LYS211
3.489
THR212
2.073
HIS214
3.222
LEU294
2.763
VAL295
2.812
TYR348
4.535
ASN382
2.184
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Crystal Structure of Aspirin-Acetylated Human Cyclooxygenase-2: Insight into the Formation of Products with Reversed Stereochemistry. Biochemistry. 2016 Mar 1;55(8):1226-38. | ||||
| REF 2 | Substrate-selective Inhibition of Cyclooxygeanse-2 by Fenamic Acid Derivatives Is Dependent on Peroxide Tone. J Biol Chem. 2016 Jul 15;291(29):15069-81. | ||||
| REF 3 | Crystal structure of rofecoxib bound to human cyclooxygenase-2. Acta Crystallogr F Struct Biol Commun. 2016 Oct 1;72(Pt 10):772-776. | ||||
If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.