|
|
1)
|
chain |
A |
residue |
94 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
96 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 301
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
119 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 301
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
4 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 302
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
64 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 302
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
17 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 303
|
source |
: AC3
|
|
7)
|
chain |
A |
residue |
174 |
type |
|
sequence |
D
|
description |
binding site for residue ZN A 304
|
source |
: AC4
|
|
8)
|
chain |
A |
residue |
34 |
type |
|
sequence |
D
|
description |
binding site for residue ZN A 305
|
source |
: AC5
|
|
9)
|
chain |
A |
residue |
36 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 305
|
source |
: AC5
|
|
10)
|
chain |
A |
residue |
186 |
type |
|
sequence |
E
|
description |
binding site for residue ZN A 306
|
source |
: AC6
|
|
11)
|
chain |
A |
residue |
52 |
type |
|
sequence |
D
|
description |
binding site for residue ZN A 307
|
source |
: AC7
|
|
12)
|
chain |
A |
residue |
15 |
type |
|
sequence |
H
|
description |
binding site for residue ZN A 308
|
source |
: AC8
|
|
13)
|
chain |
A |
residue |
62 |
type |
|
sequence |
N
|
description |
binding site for residue GOL A 309
|
source |
: AC9
|
|
14)
|
chain |
A |
residue |
65 |
type |
|
sequence |
A
|
description |
binding site for residue GOL A 309
|
source |
: AC9
|
|
15)
|
chain |
A |
residue |
67 |
type |
|
sequence |
N
|
description |
binding site for residue GOL A 309
|
source |
: AC9
|
|
16)
|
chain |
A |
residue |
92 |
type |
|
sequence |
Q
|
description |
binding site for residue GOL A 309
|
source |
: AC9
|
|
17)
|
chain |
A |
residue |
189 |
type |
|
sequence |
D
|
description |
binding site for residue ZN A 310
|
source |
: AD1
|
|
18)
|
chain |
A |
residue |
260 |
type |
|
sequence |
K
|
description |
binding site for residue ZN A 310
|
source |
: AD1
|
|
19)
|
chain |
A |
residue |
233 |
type |
|
sequence |
E
|
description |
binding site for residue ZN A 311
|
source |
: AD2
|
|
20)
|
chain |
A |
residue |
233 |
type |
|
sequence |
E
|
description |
binding site for residue ZN A 311
|
source |
: AD2
|
|
21)
|
chain |
A |
residue |
26 |
type |
|
sequence |
E
|
description |
binding site for residue ZN C 303
|
source |
: AE2
|
|
22)
|
chain |
A |
residue |
4 |
type |
|
sequence |
H
|
description |
binding site for residues QUJ A 303 and QVE A 304
|
source |
: AF6
|
|
23)
|
chain |
A |
residue |
169 |
type |
|
sequence |
K
|
description |
binding site for residues QUJ A 303 and QVE A 304
|
source |
: AF6
|
|
24)
|
chain |
A |
residue |
4 |
type |
|
sequence |
H
|
description |
binding site for residues QVE A 304 and QUJ A 305
|
source |
: AF7
|
|
25)
|
chain |
A |
residue |
19 |
type |
|
sequence |
D
|
description |
binding site for residues QVE A 304 and QUJ A 305
|
source |
: AF7
|
|
26)
|
chain |
A |
residue |
20 |
type |
|
sequence |
F
|
description |
binding site for residues QVE A 304 and QUJ A 305
|
source |
: AF7
|
|
27)
|
chain |
A |
residue |
169 |
type |
|
sequence |
K
|
description |
binding site for residues QVE A 304 and QUJ A 305
|
source |
: AF7
|
|
28)
|
chain |
A |
residue |
201 |
type |
|
sequence |
P
|
description |
binding site for residues QVE A 304 and QUJ A 305
|
source |
: AF7
|
|
29)
|
chain |
A |
residue |
4 |
type |
|
sequence |
H
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
30)
|
chain |
A |
residue |
5 |
type |
|
sequence |
W
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
31)
|
chain |
A |
residue |
19 |
type |
|
sequence |
D
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
32)
|
chain |
A |
residue |
20 |
type |
|
sequence |
F
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
33)
|
chain |
A |
residue |
64 |
type |
|
sequence |
H
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
34)
|
chain |
A |
residue |
201 |
type |
|
sequence |
P
|
description |
binding site for residues QUJ A 305 and QVE A 306
|
source |
: AF8
|
|
35)
|
chain |
A |
residue |
64 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
36)
|
chain |
A |
residue |
94 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
37)
|
chain |
A |
residue |
96 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
38)
|
chain |
A |
residue |
106 |
type |
catalytic |
sequence |
E
|
description |
216
|
source |
MCSA : MCSA1
|
|
39)
|
chain |
A |
residue |
119 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
40)
|
chain |
A |
residue |
198 |
type |
catalytic |
sequence |
T
|
description |
216
|
source |
MCSA : MCSA1
|
|
41)
|
chain |
A |
residue |
105-121 |
type |
prosite |
sequence |
SEHTVDKKKYAAELHLV
|
description |
ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
|
source |
prosite : PS00162
|
|
42)
|
chain |
A |
residue |
64 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
A |
residue |
94 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
44)
|
chain |
A |
residue |
96 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
45)
|
chain |
A |
residue |
119 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
46)
|
chain |
A |
residue |
198 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
47)
|
chain |
A |
residue |
7 |
type |
SITE |
sequence |
Y
|
description |
Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
48)
|
chain |
A |
residue |
62 |
type |
SITE |
sequence |
N
|
description |
Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
49)
|
chain |
A |
residue |
67 |
type |
SITE |
sequence |
N
|
description |
Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
50)
|
chain |
A |
residue |
92 |
type |
SITE |
sequence |
Q
|
description |
Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
51)
|
chain |
A |
residue |
2 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P27139
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
52)
|
chain |
A |
residue |
165 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
53)
|
chain |
A |
residue |
172 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|