eF-site ID 3oku-A
PDB Code 3oku
Chain A

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Title Human Carbonic Anhydrase II in complex with 2-Ethylestrone-3-O-sulfamate
Classification LYASE
Compound Carbonic anhydrase 2
Source Homo sapiens (Human) (CAH2_HUMAN)
Sequence A:  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 262
source : AC1
2) chain A
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC1
3) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC1
4) chain A
residue 92
type
sequence Q
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
5) chain A
residue 94
type
sequence H
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
6) chain A
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
7) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
8) chain A
residue 121
type
sequence V
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
9) chain A
residue 131
type
sequence F
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
10) chain A
residue 141
type
sequence L
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
11) chain A
residue 198
type
sequence L
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
12) chain A
residue 199
type
sequence T
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
13) chain A
residue 200
type
sequence T
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
14) chain A
residue 201
type
sequence P
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
15) chain A
residue 202
type
sequence P
description BINDING SITE FOR RESIDUE VZ4 A 263
source : AC2
16) chain A
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE DMS A 264
source : AC3
17) chain A
residue 243
type
sequence D
description BINDING SITE FOR RESIDUE DMS A 264
source : AC3
18) chain A
residue 245
type
sequence W
description BINDING SITE FOR RESIDUE DMS A 264
source : AC3
19) chain A
residue 62
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
20) chain A
residue 64
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
21) chain A
residue 65
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
22) chain A
residue 67
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
23) chain A
residue 92
type
sequence Q
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
24) chain A
residue 94
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 265
source : AC4
25) 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
26) 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
27) 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
28) chain A
residue 199
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
29) 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
30) 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
31) 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
32) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
33) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1
34) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1
35) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1
36) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1
37) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1
38) chain A
residue 199
type catalytic
sequence T
description 216
source MCSA : MCSA1
39) chain A
residue 166
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
40) chain A
residue 173
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
41) 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
42) 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

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