|
|
1)
|
chain |
A |
residue |
33 |
type |
|
sequence |
Q
|
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 |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
4)
|
chain |
A |
residue |
172 |
type |
|
sequence |
E
|
description |
ZINC BINDING SITE AT DIMER INTERFACE.
|
source |
: ZN2
|
|
5)
|
chain |
A |
residue |
60 |
type |
|
sequence |
C
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
6)
|
chain |
A |
residue |
62 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
7)
|
chain |
A |
residue |
65 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
8)
|
chain |
A |
residue |
67 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
9)
|
chain |
A |
residue |
69 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
10)
|
chain |
A |
residue |
71 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
11)
|
chain |
A |
residue |
88 |
type |
|
sequence |
I
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
12)
|
chain |
A |
residue |
92 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD2
|
|
13)
|
chain |
A |
residue |
157 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
14)
|
chain |
A |
residue |
160 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
15)
|
chain |
A |
residue |
162 |
type |
|
sequence |
F
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
16)
|
chain |
A |
residue |
174 |
type |
|
sequence |
L
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
17)
|
chain |
A |
residue |
179 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
18)
|
chain |
A |
residue |
183 |
type |
|
sequence |
M
|
description |
HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
|
source |
: HD3
|
|
19)
|
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
|
|
20)
|
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
|
|
21)
|
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
|
|
22)
|
chain |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE ZN B 301
|
source |
: AC1
|
|
23)
|
chain |
A |
residue |
172 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN B 301
|
source |
: AC1
|
|
24)
|
chain |
A |
residue |
33 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE ZN A 401
|
source |
: AC2
|
|
25)
|
chain |
A |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE ZN A 401
|
source |
: AC2
|
|
26)
|
chain |
A |
residue |
122 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
27)
|
chain |
A |
residue |
126 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
28)
|
chain |
A |
residue |
150 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
29)
|
chain |
A |
residue |
155 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
30)
|
chain |
A |
residue |
156 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
31)
|
chain |
A |
residue |
157 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
32)
|
chain |
A |
residue |
160 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
33)
|
chain |
A |
residue |
162 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
34)
|
chain |
A |
residue |
172 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
35)
|
chain |
A |
residue |
179 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
36)
|
chain |
A |
residue |
183 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE GIP A 300
|
source |
: AC3
|
|
37)
|
chain |
A |
residue |
33 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
38)
|
chain |
A |
residue |
37 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
39)
|
chain |
A |
residue |
67 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
40)
|
chain |
A |
residue |
69 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
41)
|
chain |
A |
residue |
71 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
42)
|
chain |
A |
residue |
99 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
43)
|
chain |
A |
residue |
101 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
44)
|
chain |
A |
residue |
103 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE GIP B 400
|
source |
: AC4
|
|
45)
|
chain |
A |
residue |
34 |
type |
catalytic |
sequence |
T
|
description |
32
|
source |
MCSA : MCSA1
|
|
46)
|
chain |
A |
residue |
100 |
type |
catalytic |
sequence |
L
|
description |
32
|
source |
MCSA : MCSA1
|
|
47)
|
chain |
A |
residue |
127 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA1
|
|
48)
|
chain |
A |
residue |
173 |
type |
catalytic |
sequence |
I
|
description |
32
|
source |
MCSA : MCSA1
|
|
49)
|
chain |
A |
residue |
33-54 |
type |
prosite |
sequence |
QTMLRVKDPKKSLDFYTRVLGM
|
description |
GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM
|
source |
prosite : PS00934
|
|
50)
|
chain |
A |
residue |
117-133 |
type |
prosite |
sequence |
GNSDPRGFGHIGIAVPD
|
description |
GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD
|
source |
prosite : PS00935
|
|
51)
|
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
|
|
52)
|
chain |
A |
residue |
148 |
type |
MOD_RES |
sequence |
F
|
description |
N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
53)
|
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
|
|
54)
|
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
|
|
55)
|
chain |
A |
residue |
38 |
type |
BINDING |
sequence |
V
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
56)
|
chain |
A |
residue |
104 |
type |
BINDING |
sequence |
W
|
description |
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
57)
|
chain |
A |
residue |
123 |
type |
BINDING |
sequence |
G
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
58)
|
chain |
A |
residue |
157 |
type |
BINDING |
sequence |
M
|
description |
in other chain
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
59)
|
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
|
|
60)
|
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
|
|
61)
|
chain |
A |
residue |
88 |
type |
MOD_RES |
sequence |
I
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
62)
|
chain |
A |
residue |
107 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphothreonine => ECO:0000269|PubMed:19199007
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
63)
|
chain |
A |
residue |
139 |
type |
MOD_RES |
sequence |
K
|
description |
S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
|
source |
Swiss-Prot : SWS_FT_FI9
|
|