eF-site ID 5l6t-A
PDB Code 5l6t
Chain A

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Title CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER
Classification Lyase/Inhibitor
Compound Carbonic anhydrase 2
Source (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 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 303
source : AC2
5) chain A
residue 64
type
sequence H
description binding site for residue ZN A 303
source : AC2
6) chain A
residue 62
type
sequence N
description binding site for residue GOL A 304
source : AC3
7) chain A
residue 64
type
sequence H
description binding site for residue GOL A 304
source : AC3
8) chain A
residue 199
type
sequence T
description binding site for residue GOL A 304
source : AC3
9) chain A
residue 200
type
sequence P
description binding site for residue GOL A 304
source : AC3
10) chain A
residue 17
type
sequence H
description binding site for residue ZN A 308
source : AC4
11) chain A
residue 36
type
sequence H
description binding site for residue ZN A 309
source : AC5
12) chain A
residue 34
type
sequence D
description binding site for residue ZN A 310
source : AC6
13) chain A
residue 174
type
sequence D
description binding site for residue ZN A 311
source : AC7
14) chain A
residue 238
type
sequence E
description binding site for residue ZN A 312
source : AC8
15) chain A
residue 72
type
sequence D
description binding site for residue ZN A 314
source : AD1
16) chain A
residue 171
type
sequence K
description binding site for residue ZN A 315
source : AD2
17) chain A
residue 233
type
sequence E
description binding site for residue ZN A 315
source : AD2
18) chain A
residue 35
type
sequence T
description binding site for residue GOL A 316
source : AD3
19) chain A
residue 38
type
sequence A
description binding site for residue GOL A 316
source : AD3
20) chain A
residue 191
type
sequence W
description binding site for residue GOL A 316
source : AD3
21) chain A
residue 259
type
sequence F
description binding site for residue GOL A 316
source : AD3
22) chain A
residue 260
type
sequence K
description binding site for residue GOL A 316
source : AD3
23) chain A
residue 94
type
sequence H
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
24) chain A
residue 96
type
sequence H
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
25) chain A
residue 119
type
sequence H
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
26) chain A
residue 121
type
sequence V
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
27) chain A
residue 130
type
sequence F
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
28) chain A
residue 142
type
sequence V
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
29) chain A
residue 197
type
sequence L
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
30) chain A
residue 198
type
sequence T
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
31) chain A
residue 199
type
sequence T
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
32) chain A
residue 208
type
sequence W
description binding site for residues 6H0 A 302 and QCL A 317
source : AE2
33) chain A
residue 4
type
sequence H
description binding site for residues QVS A 305 and QUK A 306
source : AE3
34) chain A
residue 19
type
sequence D
description binding site for residues QVS A 305 and QUK A 306
source : AE3
35) chain A
residue 20
type
sequence F
description binding site for residues QVS A 305 and QUK A 306
source : AE3
36) chain A
residue 4
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
37) chain A
residue 94
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
38) chain A
residue 96
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
39) chain A
residue 119
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
40) chain A
residue 4
type
sequence H
description binding site for residues QUK A 306 and QVE A 307
source : AE5
41) chain A
residue 5
type
sequence W
description binding site for residues QUK A 306 and QVE A 307
source : AE5
42) chain A
residue 19
type
sequence D
description binding site for residues QUK A 306 and QVE A 307
source : AE5
43) chain A
residue 20
type
sequence F
description binding site for residues QUK A 306 and QVE A 307
source : AE5
44) chain A
residue 64
type
sequence H
description binding site for residues QUK A 306 and QVE A 307
source : AE5
45) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1
46) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1
47) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1
48) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1
49) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1
50) chain A
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA1
51) 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
52) 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
53) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
54) chain A
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
55) 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
56) chain A
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
57) chain A
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
58) 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
59) 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
60) 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
61) 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
62) 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

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