|
|
1)
|
chain |
A |
residue |
229 |
type |
|
sequence |
D
|
description |
CATALYTIC SITE CONTAINING MUTANT E257Q
|
source |
: CAT
|
|
2)
|
chain |
A |
residue |
257 |
type |
|
sequence |
Q
|
description |
CATALYTIC SITE CONTAINING MUTANT E257Q
|
source |
: CAT
|
|
3)
|
chain |
A |
residue |
328 |
type |
|
sequence |
D
|
description |
CATALYTIC SITE CONTAINING MUTANT E257Q
|
source |
: CAT
|
|
4)
|
chain |
A |
residue |
27 |
type |
|
sequence |
D
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
5)
|
chain |
A |
residue |
29 |
type |
|
sequence |
N
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
6)
|
chain |
A |
residue |
32 |
type |
|
sequence |
N
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
7)
|
chain |
A |
residue |
33 |
type |
|
sequence |
N
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
8)
|
chain |
A |
residue |
51 |
type |
|
sequence |
G
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
9)
|
chain |
A |
residue |
53 |
type |
|
sequence |
D
|
description |
FIRST CALCIUM BINDING SITE.
|
source |
: CA1
|
|
10)
|
chain |
A |
residue |
139 |
type |
|
sequence |
N
|
description |
SECOND CALCIUM BINDING SITE.
|
source |
: CA2
|
|
11)
|
chain |
A |
residue |
190 |
type |
|
sequence |
I
|
description |
SECOND CALCIUM BINDING SITE.
|
source |
: CA2
|
|
12)
|
chain |
A |
residue |
199 |
type |
|
sequence |
D
|
description |
SECOND CALCIUM BINDING SITE.
|
source |
: CA2
|
|
13)
|
chain |
A |
residue |
233 |
type |
|
sequence |
H
|
description |
SECOND CALCIUM BINDING SITE.
|
source |
: CA2
|
|
14)
|
chain |
A |
residue |
382 |
type |
|
sequence |
S
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
15)
|
chain |
A |
residue |
616 |
type |
|
sequence |
W
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
16)
|
chain |
A |
residue |
651 |
type |
|
sequence |
K
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
17)
|
chain |
A |
residue |
662 |
type |
|
sequence |
W
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
18)
|
chain |
A |
residue |
663 |
type |
|
sequence |
E
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
19)
|
chain |
A |
residue |
667 |
type |
|
sequence |
N
|
description |
FIRST MALTOSE BINDING SITE.
|
source |
: 16
|
|
20)
|
chain |
A |
residue |
598 |
type |
|
sequence |
T
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
21)
|
chain |
A |
residue |
599 |
type |
|
sequence |
A
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
22)
|
chain |
A |
residue |
601 |
type |
|
sequence |
G
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
23)
|
chain |
A |
residue |
603 |
type |
|
sequence |
N
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
24)
|
chain |
A |
residue |
627 |
type |
|
sequence |
N
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
25)
|
chain |
A |
residue |
628 |
type |
|
sequence |
Q
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
26)
|
chain |
A |
residue |
633 |
type |
|
sequence |
Y
|
description |
SECOND MALTOSE BINDING SITE.
|
source |
: 26
|
|
27)
|
chain |
A |
residue |
301 |
type |
|
sequence |
Y
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
28)
|
chain |
A |
residue |
411 |
type |
|
sequence |
E
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
29)
|
chain |
A |
residue |
412 |
type |
|
sequence |
R
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
30)
|
chain |
A |
residue |
413 |
type |
|
sequence |
W
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
31)
|
chain |
A |
residue |
414 |
type |
|
sequence |
I
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
32)
|
chain |
A |
residue |
446 |
type |
|
sequence |
G
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
33)
|
chain |
A |
residue |
448 |
type |
|
sequence |
V
|
description |
THIRD MALTOSE BINDING SITE. THIS SITE ALSO INCLUDES RESIDUES SER 537, ALA 539, AND ASP 540 FROM A SYMMETRY-RELATED MOLECULE.
|
source |
: 36
|
|
34)
|
chain |
A |
residue |
227 |
type |
catalytic |
sequence |
R
|
description |
45
|
source |
MCSA : MCSA1
|
|
35)
|
chain |
A |
residue |
229 |
type |
catalytic |
sequence |
D
|
description |
45
|
source |
MCSA : MCSA1
|
|
36)
|
chain |
A |
residue |
257 |
type |
catalytic |
sequence |
Q
|
description |
45
|
source |
MCSA : MCSA1
|
|
37)
|
chain |
A |
residue |
327 |
type |
catalytic |
sequence |
H
|
description |
45
|
source |
MCSA : MCSA1
|
|
38)
|
chain |
A |
residue |
328 |
type |
catalytic |
sequence |
D
|
description |
45
|
source |
MCSA : MCSA1
|
|
39)
|
chain |
A |
residue |
229 |
type |
ACT_SITE |
sequence |
D
|
description |
Nucleophile
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
40)
|
chain |
A |
residue |
257 |
type |
ACT_SITE |
sequence |
Q
|
description |
Proton donor
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
41)
|
chain |
A |
residue |
145 |
type |
BINDING |
sequence |
S
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
42)
|
chain |
A |
residue |
190 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
43)
|
chain |
A |
residue |
193 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
44)
|
chain |
A |
residue |
199 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
45)
|
chain |
A |
residue |
227 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
46)
|
chain |
A |
residue |
232 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
47)
|
chain |
A |
residue |
233 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
48)
|
chain |
A |
residue |
315 |
type |
BINDING |
sequence |
A
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
49)
|
chain |
A |
residue |
327 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
50)
|
chain |
A |
residue |
371 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
51)
|
chain |
A |
residue |
375 |
type |
BINDING |
sequence |
R
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
52)
|
chain |
A |
residue |
577 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
53)
|
chain |
A |
residue |
51 |
type |
BINDING |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
54)
|
chain |
A |
residue |
53 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
55)
|
chain |
A |
residue |
100 |
type |
BINDING |
sequence |
Y
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
56)
|
chain |
A |
residue |
139 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
57)
|
chain |
A |
residue |
140 |
type |
BINDING |
sequence |
H
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
58)
|
chain |
A |
residue |
27 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
59)
|
chain |
A |
residue |
29 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
60)
|
chain |
A |
residue |
32 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
61)
|
chain |
A |
residue |
33 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
62)
|
chain |
A |
residue |
328 |
type |
SITE |
sequence |
D
|
description |
Transition state stabilizer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|