eF-site ID 1bnv-A
PDB Code 1bnv
Chain A

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Title CARBONIC ANHYDRASE II INHIBITOR
Classification LYASE
Compound CARBONIC ANHYDRASE
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
Description


Functional site
1) chain A
residue 94
type
sequence H
description ACTIVE SITE WITH CATALYTIC ZINC ION
source : ZN
2) chain A
residue 96
type
sequence H
description ACTIVE SITE WITH CATALYTIC ZINC ION
source : ZN
3) chain A
residue 119
type
sequence H
description ACTIVE SITE WITH CATALYTIC ZINC ION
source : ZN
4) chain A
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE HG A 263
source : AC1
5) chain A
residue 137
type
sequence Q
description BINDING SITE FOR RESIDUE HG A 263
source : AC1
6) chain A
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE HG A 263
source : AC1
7) chain A
residue 206
type
sequence C
description BINDING SITE FOR RESIDUE HG A 263
source : AC1
8) chain A
residue 94
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC2
9) chain A
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC2
10) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC2
11) chain A
residue 92
type
sequence Q
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
12) chain A
residue 94
type
sequence H
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
13) chain A
residue 96
type
sequence H
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
14) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
15) chain A
residue 131
type
sequence F
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
16) chain A
residue 198
type
sequence L
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
17) chain A
residue 199
type
sequence T
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
18) chain A
residue 200
type
sequence T
description BINDING SITE FOR RESIDUE AL7 A 555
source : AC3
19) chain A
residue 65
type ACT_SITE
sequence A
description Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI1
20) chain A
residue 65
type catalytic
sequence A
description 216
source MCSA : MCSA1
21) chain A
residue 95
type catalytic
sequence F
description 216
source MCSA : MCSA1
22) chain A
residue 97
type catalytic
sequence W
description 216
source MCSA : MCSA1
23) chain A
residue 107
type catalytic
sequence H
description 216
source MCSA : MCSA1
24) chain A
residue 120
type catalytic
sequence L
description 216
source MCSA : MCSA1
25) chain A
residue 200
type catalytic
sequence T
description 216
source MCSA : MCSA1
26) chain A
residue 63
type SITE
sequence G
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
27) chain A
residue 68
type SITE
sequence V
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 93
type SITE
sequence F
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
29) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
30) chain A
residue 200
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
31) chain A
residue 8
type SITE
sequence G
description Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI5
32) chain A
residue 167
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
33) chain A
residue 174
type MOD_RES
sequence A
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
34) chain A
residue 95
type BINDING
sequence F
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
35) chain A
residue 97
type BINDING
sequence W
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
36) chain A
residue 120
type BINDING
sequence L
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

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