eF-site ID 4cox-ABCD
PDB Code 4cox
Chain A, B, C, D

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Title CYCLOOXYGENASE-2 (PROSTAGLANDIN SYNTHASE-2) COMPLEXED WITH A NON-SELECTIVE INHIBITOR, INDOMETHACIN
Classification OXIDOREDUCTASE
Compound CYCLOOXYGENASE-2
Source (PGH2_MOUSE)
Sequence A:  ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
B:  ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
C:  ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
D:  ANPCCSNPCQNRGECMSTGFDQYKCDCTRTGFYGENCTTP
EFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNNIPFLRSL
IMKYVLTSRSYLIDSPPTYNVHYGYKSWEAFSNLSYYTRA
LPPVADDCPTPMGVKGNKELPDSKEVLEKVLLRREFIPDP
QGSNMMFAFFAQHFTHQFFKTDHKRGPGFTRGLGHGVDLN
HIYGETLDRQHKLRLFKDGKLKYQVIGGEVYPPTVKDTQV
EMIYPPHIPENLQFAVGQEVFGLVPGLMMYATIWLREHQR
VCDILKQEHPEWGDEQLFQTSKLILIGETIKIVIEDYVQH
LSGYHFKLKFDPELLFNQQFQYQNRIASEFNTLYHWHPLL
PDTFNIEDQEYSFKQFLYNNSILLEHGLTQFVESFTRQIA
GRVAGGRNVPIAVQAVAKASIDQSREMKYQSLNEYRKRFS
LKPYTSFEELTGEKEMAAELKALYSDIDVMELYPALLVEK
PRPDAIFGETMVELGAPFSLKGLMGNPICSPQYWKPSTFG
GEVGFKIINTASIQSLICNNVKGCPFTSFNVQ
Description


Functional site

1) chain A
residue 385
type
sequence Y
description TYR 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.
source : CAT

2) chain A
residue 530
type
sequence S
description SER 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).
source : ACE

3) chain A
residue 388
type
sequence H
description HIS 388 IS THE AXIAL LIGAND TO THE HEME.
source : HEM

4) chain A
residue 120
type
sequence R
description ARGININE 120 IS BELIEVED TO ANCHOR THE CARBOXYLATE OF THE SUBSTRATE BY FORMING AN ION-PAIR.
source : SUB

5) chain A
residue 203
type catalytic
sequence Q
description 37
source MCSA : MCSA1

6) chain A
residue 207
type catalytic
sequence H
description 37
source MCSA : MCSA1

7) chain A
residue 384
type catalytic
sequence L
description 37
source MCSA : MCSA1

8) chain A
residue 385
type catalytic
sequence Y
description 37
source MCSA : MCSA1

9) chain A
residue 388
type catalytic
sequence H
description 37
source MCSA : MCSA1

10) chain A
residue 526
type catalytic
sequence G
description 37
source MCSA : MCSA1

11) chain A
residue 530
type catalytic
sequence S
description 37
source MCSA : MCSA1

12) chain B
residue 203
type catalytic
sequence Q
description 37
source MCSA : MCSA2

13) chain B
residue 207
type catalytic
sequence H
description 37
source MCSA : MCSA2

14) chain B
residue 384
type catalytic
sequence L
description 37
source MCSA : MCSA2

15) chain B
residue 385
type catalytic
sequence Y
description 37
source MCSA : MCSA2

16) chain B
residue 388
type catalytic
sequence H
description 37
source MCSA : MCSA2

17) chain B
residue 526
type catalytic
sequence G
description 37
source MCSA : MCSA2

18) chain B
residue 530
type catalytic
sequence S
description 37
source MCSA : MCSA2

19) chain C
residue 203
type catalytic
sequence Q
description 37
source MCSA : MCSA3

20) chain C
residue 207
type catalytic
sequence H
description 37
source MCSA : MCSA3

21) chain C
residue 384
type catalytic
sequence L
description 37
source MCSA : MCSA3

22) chain C
residue 385
type catalytic
sequence Y
description 37
source MCSA : MCSA3

23) chain C
residue 388
type catalytic
sequence H
description 37
source MCSA : MCSA3

24) chain C
residue 526
type catalytic
sequence G
description 37
source MCSA : MCSA3

25) chain C
residue 530
type catalytic
sequence S
description 37
source MCSA : MCSA3

26) chain D
residue 203
type catalytic
sequence Q
description 37
source MCSA : MCSA4

27) chain D
residue 207
type catalytic
sequence H
description 37
source MCSA : MCSA4

28) chain D
residue 384
type catalytic
sequence L
description 37
source MCSA : MCSA4

29) chain D
residue 385
type catalytic
sequence Y
description 37
source MCSA : MCSA4

30) chain D
residue 388
type catalytic
sequence H
description 37
source MCSA : MCSA4

31) chain D
residue 526
type catalytic
sequence G
description 37
source MCSA : MCSA4

32) chain D
residue 530
type catalytic
sequence S
description 37
source MCSA : MCSA4

33) chain A
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI10

34) chain B
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI10

35) chain C
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI10

36) chain D
residue 144
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI10

37) chain A
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI11

38) chain B
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI11

39) chain C
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI11

40) chain D
residue 410
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3OLT, ECO:0007744|PDB:3OLU, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI11

41) chain A
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
source Swiss-Prot : SWS_FT_FI7

42) chain B
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
source Swiss-Prot : SWS_FT_FI7

43) chain C
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
source Swiss-Prot : SWS_FT_FI7

44) chain D
residue 540
type MOD_RES
sequence C
description S-nitrosocysteine => ECO:0000250|UniProtKB:P35354
source Swiss-Prot : SWS_FT_FI7

45) chain A
residue 579
type MOD_RES
sequence S
description O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
source Swiss-Prot : SWS_FT_FI8

46) chain B
residue 579
type MOD_RES
sequence S
description O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
source Swiss-Prot : SWS_FT_FI8

47) chain C
residue 579
type MOD_RES
sequence S
description O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
source Swiss-Prot : SWS_FT_FI8

48) chain D
residue 579
type MOD_RES
sequence S
description O-acetylserine; by SPHK1 => ECO:0000269|PubMed:29662056
source Swiss-Prot : SWS_FT_FI8

49) chain A
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI9

50) chain B
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI9

51) chain C
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI9

52) chain D
residue 68
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10811226, ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8349699, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CVU, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1DDX, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3HS5, ECO:0007744|PDB:3HS6, ECO:0007744|PDB:3HS7, ECO:0007744|PDB:3KRK, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MDL, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NT1, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:3QH0, ECO:0007744|PDB:3QMO, ECO:0007744|PDB:3TZI, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4E1G, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4OTJ, ECO:0007744|PDB:4OTY, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:4RRW, ECO:0007744|PDB:4RRX, ECO:0007744|PDB:4RRY, ECO:0007744|PDB:4RRZ, ECO:0007744|PDB:4RS0, ECO:0007744|PDB:4RUT, ECO:0007744|PDB:4Z0L, ECO:0007744|PDB:5COX, ECO:0007744|PDB:5FDQ, ECO:0007744|PDB:5JVY, ECO:0007744|PDB:5JVZ, ECO:0007744|PDB:5JW1, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI9

53) chain A
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI5

54) chain B
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI5

55) chain C
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI5

56) chain D
residue 530
type SITE
sequence S
description Aspirin-acetylated serine
source Swiss-Prot : SWS_FT_FI5

57) chain A
residue 388
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI4

58) chain B
residue 388
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI4

59) chain C
residue 388
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI4

60) chain D
residue 388
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:8967954, ECO:0007744|PDB:1CX2, ECO:0007744|PDB:1PXX, ECO:0007744|PDB:3LN0, ECO:0007744|PDB:3LN1, ECO:0007744|PDB:3MQE, ECO:0007744|PDB:3NTB, ECO:0007744|PDB:3NTG, ECO:0007744|PDB:3PGH, ECO:0007744|PDB:4COX, ECO:0007744|PDB:4FM5, ECO:0007744|PDB:4M10, ECO:0007744|PDB:4M11, ECO:0007744|PDB:4PH9, ECO:0007744|PDB:5COX, ECO:0007744|PDB:6COX
source Swiss-Prot : SWS_FT_FI4

61) chain A
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI2

62) chain B
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI2

63) chain C
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI2

64) chain D
residue 385
type ACT_SITE
sequence Y
description For cyclooxygenase activity => ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI2

65) chain A
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI1

66) chain B
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI1

67) chain C
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI1

68) chain D
residue 207
type ACT_SITE
sequence H
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298, ECO:0000269|PubMed:20463020
source Swiss-Prot : SWS_FT_FI1

69) chain A
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

70) chain A
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

71) chain B
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

72) chain B
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

73) chain C
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

74) chain C
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

75) chain D
residue 120
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3

76) chain D
residue 355
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:20463020, ECO:0007744|PDB:3KRK
source Swiss-Prot : SWS_FT_FI3


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