|
eF-site ID
|
4z1k-A |
PDB Code
|
4z1k |
Chain
|
A |
|
click to enlarge
|
|
Title
|
Carbonic anhydrase inhibitors: Design and synthesis of new heteroaryl-N-carbonylbenzenesulfonamides targeting druggable human carbonic anhydrase isoforms (hCA VII, hCA IX, and hCA XIV) |
Classification
|
LYASE |
Compound
|
Carbonic anhydrase 2 |
Source
|
Homo sapiens (Human) (CAH2_HUMAN) |
|
Sequence
|
A: |
HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
|
|
Description
|
|
Functional site
|
|
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 |
92 |
type |
|
sequence |
Q
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
94 |
type |
|
sequence |
H
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
96 |
type |
|
sequence |
H
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
119 |
type |
|
sequence |
H
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
121 |
type |
|
sequence |
V
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
130 |
type |
|
sequence |
F
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
197 |
type |
|
sequence |
L
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
198 |
type |
|
sequence |
T
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
199 |
type |
|
sequence |
T
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
208 |
type |
|
sequence |
W
|
description |
binding site for residue 4KB A 302
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
64 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
15)
|
chain |
A |
residue |
94 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
A |
residue |
96 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
A |
residue |
106 |
type |
catalytic |
sequence |
E
|
description |
216
|
source |
MCSA : MCSA1
|
|
18)
|
chain |
A |
residue |
119 |
type |
catalytic |
sequence |
H
|
description |
216
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
A |
residue |
198 |
type |
catalytic |
sequence |
T
|
description |
216
|
source |
MCSA : MCSA1
|
|
20)
|
chain |
A |
residue |
105-121 |
type |
prosite |
sequence |
SEHTVDKKKYAAELHLV
|
description |
ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
|
source |
prosite : PS00162
|
|
21)
|
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
|
|
22)
|
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
|
|
23)
|
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
|
|
24)
|
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
|
|
25)
|
chain |
A |
residue |
198 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
26)
|
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
|
|
27)
|
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
|
|
28)
|
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
|
|
29)
|
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
|
|
30)
|
chain |
A |
residue |
165 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
31)
|
chain |
A |
residue |
172 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
|
|