|
|
1)
|
chain |
A |
residue |
144 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
2)
|
chain |
A |
residue |
410 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
3)
|
chain |
B |
residue |
144 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
4)
|
chain |
B |
residue |
410 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0000269|PubMed:27710942, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKR, ECO:0007744|PDB:5IKT, ECO:0007744|PDB:5IKV, ECO:0007744|PDB:5KIR
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
5)
|
chain |
A |
residue |
530 |
type |
SITE |
sequence |
S
|
description |
Aspirin-acetylated serine => ECO:0000269|PubMed:26859324
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
6)
|
chain |
B |
residue |
530 |
type |
SITE |
sequence |
S
|
description |
Aspirin-acetylated serine => ECO:0000269|PubMed:26859324
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
7)
|
chain |
A |
residue |
540 |
type |
MOD_RES |
sequence |
C
|
description |
S-nitrosocysteine => ECO:0000305|PubMed:16373578
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
8)
|
chain |
B |
residue |
540 |
type |
MOD_RES |
sequence |
C
|
description |
S-nitrosocysteine => ECO:0000305|PubMed:16373578
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
9)
|
chain |
A |
residue |
579 |
type |
MOD_RES |
sequence |
S
|
description |
O-acetylserine => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
10)
|
chain |
B |
residue |
579 |
type |
MOD_RES |
sequence |
S
|
description |
O-acetylserine => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
11)
|
chain |
A |
residue |
68 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKT
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
12)
|
chain |
B |
residue |
68 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:26859324, ECO:0000269|PubMed:27226593, ECO:0007744|PDB:5F19, ECO:0007744|PDB:5F1A, ECO:0007744|PDB:5IKQ, ECO:0007744|PDB:5IKT
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
13)
|
chain |
A |
residue |
388 |
type |
BINDING |
sequence |
H
|
description |
axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
14)
|
chain |
B |
residue |
388 |
type |
BINDING |
sequence |
H
|
description |
axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00298
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
15)
|
chain |
A |
residue |
207 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
B |
residue |
207 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00298
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
385 |
type |
ACT_SITE |
sequence |
Y
|
description |
For cyclooxygenase activity => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
B |
residue |
385 |
type |
ACT_SITE |
sequence |
Y
|
description |
For cyclooxygenase activity => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
120 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
355 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
B |
residue |
120 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
B |
residue |
355 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000250|UniProtKB:Q05769
|
source |
Swiss-Prot : SWS_FT_FI3
|
|