|
|
1)
|
chain |
A |
residue |
82 |
type |
|
sequence |
N
|
description |
binding site for residue IOD A 201
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
146 |
type |
|
sequence |
S
|
description |
binding site for residue IOD A 201
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
184 |
type |
|
sequence |
S
|
description |
binding site for residue IOD A 202
|
source |
: AC2
|
|
4)
|
chain |
A |
residue |
123 |
type |
|
sequence |
V
|
description |
binding site for residue IOD A 203
|
source |
: AC3
|
|
5)
|
chain |
A |
residue |
82 |
type |
|
sequence |
N
|
description |
binding site for residue TRS A 204
|
source |
: AC4
|
|
6)
|
chain |
A |
residue |
92 |
type |
|
sequence |
N
|
description |
binding site for residue TRS A 204
|
source |
: AC4
|
|
7)
|
chain |
A |
residue |
145 |
type |
|
sequence |
R
|
description |
binding site for residue TRS A 204
|
source |
: AC4
|
|
8)
|
chain |
A |
residue |
146 |
type |
|
sequence |
S
|
description |
binding site for residue TRS A 204
|
source |
: AC4
|
|
9)
|
chain |
A |
residue |
83-93 |
type |
prosite |
sequence |
PLIEYYIVENF
|
description |
GH11_1 Glycosyl hydrolases family 11 (GH11) active site signature 1. PLiEYYIVEnF
|
source |
prosite : PS00776
|
|
10)
|
chain |
A |
residue |
174-185 |
type |
prosite |
sequence |
VAVEGYFSSGSA
|
description |
GH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. VavEGYFSSGsA
|
source |
prosite : PS00777
|
|
11)
|
chain |
A |
residue |
87 |
type |
ACT_SITE |
sequence |
Y
|
description |
Nucleophile => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
178 |
type |
ACT_SITE |
sequence |
G
|
description |
Proton donor => ECO:0000269|PubMed:26392527, ECO:0000305|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
13)
|
chain |
A |
residue |
74 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
14)
|
chain |
A |
residue |
78 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
A |
residue |
89 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
A |
residue |
123 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
A |
residue |
127 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
A |
residue |
137 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
19)
|
chain |
A |
residue |
172 |
type |
BINDING |
sequence |
Q
|
description |
BINDING => ECO:0000269|PubMed:24419374
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
39 |
type |
CARBOHYD |
sequence |
W
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
21)
|
chain |
A |
residue |
62 |
type |
CARBOHYD |
sequence |
F
|
description |
N-linked (GlcNAc...) asparagine => ECO:0000255
|
source |
Swiss-Prot : SWS_FT_FI5
|
|