|
|
1)
|
chain |
B |
residue |
120 |
type |
|
sequence |
R
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
2)
|
chain |
B |
residue |
355 |
type |
|
sequence |
Y
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
3)
|
chain |
B |
residue |
385 |
type |
|
sequence |
Y
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
4)
|
chain |
B |
residue |
387 |
type |
|
sequence |
W
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
5)
|
chain |
B |
residue |
523 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
6)
|
chain |
B |
residue |
530 |
type |
|
sequence |
S
|
description |
HYDROPHOBIC CHANNEL RESPONSIBLE FOR CYCLOOGENASE ACTIVITY
|
source |
: COB
|
|
7)
|
chain |
B |
residue |
207 |
type |
|
sequence |
H
|
description |
HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
|
source |
: POB
|
|
8)
|
chain |
B |
residue |
388 |
type |
|
sequence |
H
|
description |
HEME POCKET RESPONSIBLE FOR PEROXIDASE ACTIVITY
|
source |
: POB
|
|
9)
|
chain |
B |
residue |
74-82 |
type |
TRANSMEM |
sequence |
IWTWLRTTL
|
description |
Helical
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
chain |
B |
residue |
86-92 |
type |
TRANSMEM |
sequence |
PSFIHFL
|
description |
Helical
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
11)
|
chain |
B |
residue |
97-105 |
type |
TRANSMEM |
sequence |
RWLWDFVNA
|
description |
Helical
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
B |
residue |
108-122 |
type |
TRANSMEM |
sequence |
IRDTLMRLVLTVRSN
|
description |
Helical
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
13)
|
chain |
B |
residue |
207 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton acceptor
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
B |
residue |
385 |
type |
ACT_SITE |
sequence |
Y
|
description |
For cyclooxygenase activity => ECO:0000269|PubMed:2122967
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
B |
residue |
388 |
type |
BINDING |
sequence |
H
|
description |
axial binding residue
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
16)
|
chain |
B |
residue |
104 |
type |
SITE |
sequence |
N
|
description |
Not glycosylated => ECO:0000269|PubMed:8349699
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
17)
|
chain |
B |
residue |
530 |
type |
SITE |
sequence |
S
|
description |
Aspirin-acetylated serine
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
18)
|
chain |
B |
residue |
68 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
19)
|
chain |
B |
residue |
144 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
20)
|
chain |
B |
residue |
410 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8349699
|
source |
Swiss-Prot : SWS_FT_FI7
|
|