eF-site ID 5doh-AB
PDB Code 5doh
Chain A, B

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Title Crystal structure of human carbonic anhydrase isozyme II with 2-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)thio]benzenesulfonamide
Classification LYASE
Compound Carbonic anhydrase 2
Source (CAH2_HUMAN)
Sequence A:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
B:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
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 149
type
sequence K
description binding site for residue BCN A 302
source : AC2
5) chain A
residue 213
type
sequence K
description binding site for residue BCN A 302
source : AC2
6) chain A
residue 214
type
sequence E
description binding site for residue BCN A 302
source : AC2
7) chain A
residue 215
type
sequence P
description binding site for residue BCN A 302
source : AC2
8) chain A
residue 7
type
sequence Y
description binding site for residue DMS A 303
source : AC3
9) chain A
residue 243
type
sequence D
description binding site for residue DMS A 303
source : AC3
10) chain A
residue 245
type
sequence W
description binding site for residue DMS A 303
source : AC3
11) chain A
residue 7
type
sequence Y
description binding site for residue 5DU A 304
source : AC4
12) chain A
residue 64
type
sequence H
description binding site for residue 5DU A 304
source : AC4
13) chain A
residue 65
type
sequence A
description binding site for residue 5DU A 304
source : AC4
14) chain A
residue 92
type
sequence Q
description binding site for residue 5DU A 304
source : AC4
15) chain A
residue 94
type
sequence H
description binding site for residue 5DU A 304
source : AC4
16) chain A
residue 96
type
sequence H
description binding site for residue 5DU A 304
source : AC4
17) chain A
residue 119
type
sequence H
description binding site for residue 5DU A 304
source : AC4
18) chain A
residue 121
type
sequence V
description binding site for residue 5DU A 304
source : AC4
19) chain A
residue 131
type
sequence F
description binding site for residue 5DU A 304
source : AC4
20) chain A
residue 141
type
sequence L
description binding site for residue 5DU A 304
source : AC4
21) chain A
residue 198
type
sequence L
description binding site for residue 5DU A 304
source : AC4
22) chain A
residue 199
type
sequence T
description binding site for residue 5DU A 304
source : AC4
23) chain A
residue 200
type
sequence T
description binding site for residue 5DU A 304
source : AC4
24) chain B
residue 94
type
sequence H
description binding site for residue ZN B 301
source : AC5
25) chain B
residue 96
type
sequence H
description binding site for residue ZN B 301
source : AC5
26) chain B
residue 119
type
sequence H
description binding site for residue ZN B 301
source : AC5
27) chain B
residue 149
type
sequence K
description binding site for residue BCN B 302
source : AC6
28) chain B
residue 213
type
sequence K
description binding site for residue BCN B 302
source : AC6
29) chain B
residue 215
type
sequence P
description binding site for residue BCN B 302
source : AC6
30) chain B
residue 7
type
sequence Y
description binding site for residue DMS B 303
source : AC7
31) chain B
residue 243
type
sequence D
description binding site for residue DMS B 303
source : AC7
32) chain B
residue 245
type
sequence W
description binding site for residue DMS B 303
source : AC7
33) chain B
residue 247
type
sequence P
description binding site for residue DMS B 303
source : AC7
34) chain B
residue 7
type
sequence Y
description binding site for residue 5DU B 304
source : AC8
35) chain B
residue 64
type
sequence H
description binding site for residue 5DU B 304
source : AC8
36) chain B
residue 65
type
sequence A
description binding site for residue 5DU B 304
source : AC8
37) chain B
residue 92
type
sequence Q
description binding site for residue 5DU B 304
source : AC8
38) chain B
residue 94
type
sequence H
description binding site for residue 5DU B 304
source : AC8
39) chain B
residue 96
type
sequence H
description binding site for residue 5DU B 304
source : AC8
40) chain B
residue 119
type
sequence H
description binding site for residue 5DU B 304
source : AC8
41) chain B
residue 121
type
sequence V
description binding site for residue 5DU B 304
source : AC8
42) chain B
residue 131
type
sequence F
description binding site for residue 5DU B 304
source : AC8
43) chain B
residue 141
type
sequence L
description binding site for residue 5DU B 304
source : AC8
44) chain B
residue 198
type
sequence L
description binding site for residue 5DU B 304
source : AC8
45) chain B
residue 199
type
sequence T
description binding site for residue 5DU B 304
source : AC8
46) chain B
residue 200
type
sequence T
description binding site for residue 5DU B 304
source : AC8
47) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1
48) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1
49) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1
50) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1
51) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1
52) chain A
residue 199
type catalytic
sequence T
description 216
source MCSA : MCSA1
53) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2
54) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2
55) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2
56) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2
57) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2
58) chain B
residue 199
type catalytic
sequence T
description 216
source MCSA : MCSA2
59) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
60) 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
61) chain B
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
62) 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
63) chain B
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
64) 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
65) 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
66) chain B
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
67) chain B
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
68) chain A
residue 199
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
69) chain B
residue 199
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
70) 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
71) chain B
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
72) 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
73) 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
74) chain B
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
75) chain B
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
76) 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
77) chain B
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
78) chain A
residue 166
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
79) chain A
residue 173
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
80) chain B
residue 166
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
81) chain B
residue 173
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

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