|
|
1)
|
chain |
A |
residue |
33 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN1
|
|
2)
|
chain |
A |
residue |
99 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN1
|
|
3)
|
chain |
B |
residue |
126 |
type |
|
sequence |
H
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN1
|
|
4)
|
chain |
B |
residue |
172 |
type |
|
sequence |
Q
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN1
|
|
5)
|
chain |
B |
residue |
33 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
6)
|
chain |
B |
residue |
99 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
7)
|
chain |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
8)
|
chain |
A |
residue |
172 |
type |
|
sequence |
Q
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
9)
|
chain |
C |
residue |
33 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN3
|
|
10)
|
chain |
C |
residue |
99 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN3
|
|
11)
|
chain |
D |
residue |
126 |
type |
|
sequence |
H
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN3
|
|
12)
|
chain |
D |
residue |
172 |
type |
|
sequence |
Q
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN3
|
|
13)
|
chain |
D |
residue |
33 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN4
|
|
14)
|
chain |
D |
residue |
99 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN4
|
|
15)
|
chain |
C |
residue |
126 |
type |
|
sequence |
H
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN4
|
|
16)
|
chain |
C |
residue |
172 |
type |
|
sequence |
Q
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN4
|
|
17)
|
chain |
A |
residue |
60 |
type |
|
sequence |
C
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
18)
|
chain |
A |
residue |
62 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
19)
|
chain |
A |
residue |
65 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
20)
|
chain |
A |
residue |
67 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
21)
|
chain |
A |
residue |
69 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
22)
|
chain |
A |
residue |
71 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
23)
|
chain |
A |
residue |
88 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
24)
|
chain |
A |
residue |
92 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
25)
|
chain |
B |
residue |
157 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
26)
|
chain |
B |
residue |
160 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
27)
|
chain |
B |
residue |
162 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
28)
|
chain |
B |
residue |
174 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
29)
|
chain |
B |
residue |
179 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
30)
|
chain |
B |
residue |
183 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
31)
|
chain |
B |
residue |
60 |
type |
|
sequence |
C
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
32)
|
chain |
B |
residue |
62 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
33)
|
chain |
B |
residue |
65 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
34)
|
chain |
B |
residue |
67 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
35)
|
chain |
B |
residue |
69 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
36)
|
chain |
B |
residue |
71 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
37)
|
chain |
B |
residue |
88 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
38)
|
chain |
B |
residue |
92 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
39)
|
chain |
A |
residue |
157 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
40)
|
chain |
A |
residue |
160 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
41)
|
chain |
A |
residue |
162 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
42)
|
chain |
A |
residue |
174 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
43)
|
chain |
A |
residue |
179 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
44)
|
chain |
A |
residue |
183 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
45)
|
chain |
C |
residue |
60 |
type |
|
sequence |
C
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
46)
|
chain |
C |
residue |
62 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
47)
|
chain |
C |
residue |
65 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
48)
|
chain |
C |
residue |
67 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
49)
|
chain |
C |
residue |
69 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
50)
|
chain |
C |
residue |
71 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
51)
|
chain |
C |
residue |
88 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
52)
|
chain |
C |
residue |
92 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
53)
|
chain |
D |
residue |
157 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
54)
|
chain |
D |
residue |
160 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
55)
|
chain |
D |
residue |
162 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
56)
|
chain |
D |
residue |
174 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
57)
|
chain |
D |
residue |
179 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
58)
|
chain |
D |
residue |
183 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD4
|
|
59)
|
chain |
D |
residue |
60 |
type |
|
sequence |
C
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
60)
|
chain |
D |
residue |
62 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
61)
|
chain |
D |
residue |
65 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
62)
|
chain |
D |
residue |
67 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
63)
|
chain |
D |
residue |
69 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
64)
|
chain |
D |
residue |
71 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
65)
|
chain |
D |
residue |
88 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
66)
|
chain |
D |
residue |
92 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
67)
|
chain |
C |
residue |
157 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
68)
|
chain |
C |
residue |
160 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
69)
|
chain |
C |
residue |
162 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
70)
|
chain |
C |
residue |
174 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
71)
|
chain |
C |
residue |
179 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
72)
|
chain |
C |
residue |
183 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD5
|
|
73)
|
chain |
B |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH2
|
|
74)
|
chain |
B |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH2
|
|
75)
|
chain |
A |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH2
|
|
76)
|
chain |
A |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH1
|
|
77)
|
chain |
A |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH1
|
|
78)
|
chain |
B |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH1
|
|
79)
|
chain |
D |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH4
|
|
80)
|
chain |
D |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH4
|
|
81)
|
chain |
C |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
|
source |
: GH4
|
|
82)
|
chain |
C |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH3
|
|
83)
|
chain |
C |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH3
|
|
84)
|
chain |
D |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
|
source |
: GH3
|
|
85)
|
chain |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN A 201
|
source |
: AC1
|
|
86)
|
chain |
A |
residue |
172 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE ZN A 201
|
source |
: AC1
|
|
87)
|
chain |
B |
residue |
33 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN A 201
|
source |
: AC1
|
|
88)
|
chain |
B |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN A 201
|
source |
: AC1
|
|
89)
|
chain |
A |
residue |
33 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN B 201
|
source |
: AC2
|
|
90)
|
chain |
A |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN B 201
|
source |
: AC2
|
|
91)
|
chain |
B |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN B 201
|
source |
: AC2
|
|
92)
|
chain |
B |
residue |
172 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE ZN B 201
|
source |
: AC2
|
|
93)
|
chain |
C |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN C 201
|
source |
: AC3
|
|
94)
|
chain |
C |
residue |
172 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE ZN C 201
|
source |
: AC3
|
|
95)
|
chain |
D |
residue |
33 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN C 201
|
source |
: AC3
|
|
96)
|
chain |
D |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN C 201
|
source |
: AC3
|
|
97)
|
chain |
C |
residue |
33 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN D 201
|
source |
: AC4
|
|
98)
|
chain |
C |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN D 201
|
source |
: AC4
|
|
99)
|
chain |
D |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN D 201
|
source |
: AC4
|
|
100)
|
chain |
D |
residue |
172 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE ZN D 201
|
source |
: AC4
|
|
101)
|
chain |
A |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
102)
|
chain |
A |
residue |
157 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
103)
|
chain |
A |
residue |
162 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
104)
|
chain |
B |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
105)
|
chain |
B |
residue |
60 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
106)
|
chain |
B |
residue |
67 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
107)
|
chain |
B |
residue |
92 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
108)
|
chain |
B |
residue |
101 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
109)
|
chain |
B |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
110)
|
chain |
C |
residue |
17 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE GTX A 200
|
source |
: AC5
|
|
111)
|
chain |
A |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
112)
|
chain |
A |
residue |
60 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
113)
|
chain |
A |
residue |
67 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
114)
|
chain |
A |
residue |
101 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
115)
|
chain |
A |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
116)
|
chain |
A |
residue |
139 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
117)
|
chain |
B |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
118)
|
chain |
B |
residue |
150 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
119)
|
chain |
B |
residue |
157 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
120)
|
chain |
B |
residue |
162 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
121)
|
chain |
B |
residue |
183 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX B 200
|
source |
: AC6
|
|
122)
|
chain |
A |
residue |
17 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
123)
|
chain |
C |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
124)
|
chain |
C |
residue |
157 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
125)
|
chain |
C |
residue |
160 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
126)
|
chain |
C |
residue |
162 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
127)
|
chain |
C |
residue |
179 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
128)
|
chain |
D |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
129)
|
chain |
D |
residue |
60 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
130)
|
chain |
D |
residue |
67 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
131)
|
chain |
D |
residue |
92 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
132)
|
chain |
D |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE GTX C 200
|
source |
: AC7
|
|
133)
|
chain |
C |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
134)
|
chain |
C |
residue |
60 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
135)
|
chain |
C |
residue |
67 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
136)
|
chain |
C |
residue |
101 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
137)
|
chain |
C |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
138)
|
chain |
D |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
139)
|
chain |
D |
residue |
160 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
140)
|
chain |
D |
residue |
162 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
141)
|
chain |
D |
residue |
183 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GTX D 200
|
source |
: AC8
|
|
142)
|
chain |
A |
residue |
173 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
143)
|
chain |
B |
residue |
173 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
144)
|
chain |
C |
residue |
173 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
145)
|
chain |
D |
residue |
173 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
146)
|
chain |
A |
residue |
148 |
type |
MOD_RES |
sequence |
F
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
147)
|
chain |
B |
residue |
148 |
type |
MOD_RES |
sequence |
F
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
148)
|
chain |
C |
residue |
148 |
type |
MOD_RES |
sequence |
F
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
149)
|
chain |
D |
residue |
148 |
type |
MOD_RES |
sequence |
F
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
150)
|
chain |
A |
residue |
34 |
type |
catalytic |
sequence |
T
|
description |
32
|
source |
MCSA : MCSA1
|
|
151)
|
chain |
A |
residue |
100 |
type |
catalytic |
sequence |
L
|
description |
32
|
source |
MCSA : MCSA1
|
|
152)
|
chain |
A |
residue |
127 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA1
|
|
153)
|
chain |
A |
residue |
173 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA1
|
|
154)
|
chain |
B |
residue |
34 |
type |
catalytic |
sequence |
T
|
description |
32
|
source |
MCSA : MCSA2
|
|
155)
|
chain |
B |
residue |
100 |
type |
catalytic |
sequence |
L
|
description |
32
|
source |
MCSA : MCSA2
|
|
156)
|
chain |
B |
residue |
127 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA2
|
|
157)
|
chain |
B |
residue |
173 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA2
|
|
158)
|
chain |
C |
residue |
34 |
type |
catalytic |
sequence |
T
|
description |
32
|
source |
MCSA : MCSA3
|
|
159)
|
chain |
C |
residue |
100 |
type |
catalytic |
sequence |
L
|
description |
32
|
source |
MCSA : MCSA3
|
|
160)
|
chain |
C |
residue |
127 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA3
|
|
161)
|
chain |
C |
residue |
173 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA3
|
|
162)
|
chain |
D |
residue |
34 |
type |
catalytic |
sequence |
T
|
description |
32
|
source |
MCSA : MCSA4
|
|
163)
|
chain |
D |
residue |
100 |
type |
catalytic |
sequence |
L
|
description |
32
|
source |
MCSA : MCSA4
|
|
164)
|
chain |
D |
residue |
127 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA4
|
|
165)
|
chain |
D |
residue |
173 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA4
|
|
166)
|
chain |
A |
residue |
88 |
type |
MOD_RES |
sequence |
I
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
167)
|
chain |
B |
residue |
88 |
type |
MOD_RES |
sequence |
I
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
168)
|
chain |
C |
residue |
88 |
type |
MOD_RES |
sequence |
I
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
169)
|
chain |
D |
residue |
88 |
type |
MOD_RES |
sequence |
I
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
170)
|
chain |
A |
residue |
139 |
type |
MOD_RES |
sequence |
K
|
description |
S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
171)
|
chain |
B |
residue |
139 |
type |
MOD_RES |
sequence |
K
|
description |
S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
172)
|
chain |
C |
residue |
139 |
type |
MOD_RES |
sequence |
K
|
description |
S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
173)
|
chain |
D |
residue |
139 |
type |
MOD_RES |
sequence |
K
|
description |
S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
174)
|
chain |
A |
residue |
34 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
175)
|
chain |
A |
residue |
100 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
176)
|
chain |
B |
residue |
34 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
177)
|
chain |
B |
residue |
100 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
178)
|
chain |
C |
residue |
34 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
179)
|
chain |
C |
residue |
100 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
180)
|
chain |
D |
residue |
34 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
181)
|
chain |
D |
residue |
100 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
182)
|
chain |
A |
residue |
38 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
183)
|
chain |
A |
residue |
104 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
184)
|
chain |
B |
residue |
38 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
185)
|
chain |
B |
residue |
104 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
186)
|
chain |
C |
residue |
38 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
187)
|
chain |
C |
residue |
104 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
188)
|
chain |
D |
residue |
38 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
189)
|
chain |
D |
residue |
104 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
190)
|
chain |
A |
residue |
123 |
type |
BINDING |
sequence |
G
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
191)
|
chain |
A |
residue |
157 |
type |
BINDING |
sequence |
M
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
192)
|
chain |
B |
residue |
123 |
type |
BINDING |
sequence |
G
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
193)
|
chain |
B |
residue |
157 |
type |
BINDING |
sequence |
M
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
194)
|
chain |
C |
residue |
123 |
type |
BINDING |
sequence |
G
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
195)
|
chain |
C |
residue |
157 |
type |
BINDING |
sequence |
M
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
196)
|
chain |
D |
residue |
123 |
type |
BINDING |
sequence |
G
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
197)
|
chain |
D |
residue |
157 |
type |
BINDING |
sequence |
M
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
198)
|
chain |
A |
residue |
117-133 |
type |
prosite |
sequence |
GNSDPRGFGHIGIAVPD
|
description |
GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD
|
source |
prosite : PS00935
|
|
199)
|
chain |
A |
residue |
127 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
200)
|
chain |
A |
residue |
173 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
201)
|
chain |
B |
residue |
127 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
202)
|
chain |
B |
residue |
173 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
203)
|
chain |
C |
residue |
127 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
204)
|
chain |
C |
residue |
173 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
205)
|
chain |
D |
residue |
127 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
206)
|
chain |
D |
residue |
173 |
type |
BINDING |
sequence |
I
|
description |
in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
207)
|
chain |
B |
residue |
2 |
type |
MOD_RES |
sequence |
E
|
description |
N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
208)
|
chain |
D |
residue |
2 |
type |
MOD_RES |
sequence |
E
|
description |
N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
209)
|
chain |
A |
residue |
107 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphothreonine => ECO:0000269|PubMed:19199007
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
210)
|
chain |
B |
residue |
107 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphothreonine => ECO:0000269|PubMed:19199007
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
211)
|
chain |
C |
residue |
107 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphothreonine => ECO:0000269|PubMed:19199007
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
212)
|
chain |
D |
residue |
107 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphothreonine => ECO:0000269|PubMed:19199007
|
source |
Swiss-Prot : SWS_FT_FI8
|
|