|
|
1)
|
chain |
A |
residue |
146 |
type |
|
sequence |
S
|
description |
|
source |
: CAT
|
|
2)
|
chain |
A |
residue |
338 |
type |
|
sequence |
D
|
description |
|
source |
: CAT
|
|
3)
|
chain |
A |
residue |
397 |
type |
|
sequence |
H
|
description |
|
source |
: CAT
|
|
4)
|
chain |
A |
residue |
145 |
type |
|
sequence |
E
|
description |
|
source |
: CAT
|
|
5)
|
chain |
A |
residue |
51 |
type |
|
sequence |
N
|
description |
|
source |
: CBS
|
|
6)
|
chain |
A |
residue |
52 |
type |
|
sequence |
G
|
description |
|
source |
: CBS
|
|
7)
|
chain |
A |
residue |
145 |
type |
|
sequence |
E
|
description |
|
source |
: CBS
|
|
8)
|
chain |
A |
residue |
397 |
type |
|
sequence |
H
|
description |
|
source |
: CBS
|
|
9)
|
chain |
A |
residue |
60 |
type |
|
sequence |
T
|
description |
|
source |
: S1P
|
|
10)
|
chain |
A |
residue |
64 |
type |
|
sequence |
F
|
description |
|
source |
: S1P
|
|
11)
|
chain |
A |
residue |
65 |
type |
|
sequence |
E
|
description |
|
source |
: S1P
|
|
12)
|
chain |
A |
residue |
256 |
type |
|
sequence |
Y
|
description |
|
source |
: S1P
|
|
13)
|
chain |
A |
residue |
269 |
type |
|
sequence |
Y
|
description |
|
source |
: S1P
|
|
14)
|
chain |
A |
residue |
272 |
type |
|
sequence |
L
|
description |
|
source |
: S1P
|
|
15)
|
chain |
A |
residue |
398 |
type |
|
sequence |
M
|
description |
|
source |
: S1P
|
|
16)
|
chain |
A |
residue |
147 |
type |
|
sequence |
Y
|
description |
|
source |
: S1S
|
|
17)
|
chain |
A |
residue |
178 |
type |
|
sequence |
L
|
description |
|
source |
: S1S
|
|
18)
|
chain |
A |
residue |
245 |
type |
|
sequence |
L
|
description |
|
source |
: S1S
|
|
19)
|
chain |
A |
residue |
312 |
type |
|
sequence |
W
|
description |
|
source |
: S1S
|
|
20)
|
chain |
A |
residue |
340 |
type |
|
sequence |
I
|
description |
|
source |
: S1S
|
|
21)
|
chain |
A |
residue |
341 |
type |
|
sequence |
C
|
description |
|
source |
: S1S
|
|
22)
|
chain |
A |
residue |
13 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:28189789
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
23)
|
chain |
A |
residue |
341 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000305|DOI:10.1007/BF02907496
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
24)
|
chain |
A |
residue |
398 |
type |
BINDING |
sequence |
M
|
description |
BINDING => ECO:0000305|DOI:10.1007/BF02907496
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
25)
|
chain |
A |
residue |
87 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:15713484, ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
26)
|
chain |
A |
residue |
168 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:15713484, ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
27)
|
chain |
A |
residue |
368 |
type |
CARBOHYD |
sequence |
N
|
description |
N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:15713484, ECO:0000269|PubMed:28189789, ECO:0000269|PubMed:7727362
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
28)
|
chain |
A |
residue |
338 |
type |
ACT_SITE |
sequence |
D
|
description |
ACT_SITE => ECO:0000305|PubMed:7727362
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
29)
|
chain |
A |
residue |
397 |
type |
ACT_SITE |
sequence |
H
|
description |
ACT_SITE => ECO:0000269|PubMed:2639680, ECO:0000305|PubMed:7727362
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
30)
|
chain |
A |
residue |
146 |
type |
ACT_SITE |
sequence |
S
|
description |
ACT_SITE => ECO:0000269|PubMed:7727362, ECO:0000269|DOI:10.1007/BF02907496
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
A |
residue |
142-149 |
type |
prosite |
sequence |
IAGESYAG
|
description |
CARBOXYPEPT_SER_SER Serine carboxypeptidases, serine active site. IaGESYAG
|
source |
prosite : PS00131
|
|
32)
|
chain |
A |
residue |
387-404 |
type |
prosite |
sequence |
FTYLRVFNGGHMVPFDVP
|
description |
CARBOXYPEPT_SER_HIS Serine carboxypeptidases, histidine active site. FtyLrVfNGGHmVPfdvP
|
source |
prosite : PS00560
|
|