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

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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 B:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSQVLKFRKLNFNGEELMVDNWRPAQ
PLKNRQIKASF
Description


Functional site
1) chain B
residue 34
type
sequence D
description binding site for residue ZN A 309
source : AC5
2) chain B
residue 36
type
sequence H
description binding site for residue ZN A 310
source : AC6
3) chain B
residue 174
type
sequence D
description binding site for residue ZN A 315
source : AD2
4) chain B
residue 94
type
sequence H
description binding site for residue ZN B 302
source : AD4
5) chain B
residue 96
type
sequence H
description binding site for residue ZN B 302
source : AD4
6) chain B
residue 119
type
sequence H
description binding site for residue ZN B 302
source : AD4
7) chain B
residue 4
type
sequence H
description binding site for residue ZN B 304
source : AD5
8) chain B
residue 64
type
sequence H
description binding site for residue ZN B 304
source : AD5
9) chain B
residue 62
type
sequence N
description binding site for residue GOL B 305
source : AD6
10) chain B
residue 199
type
sequence T
description binding site for residue GOL B 305
source : AD6
11) chain B
residue 200
type
sequence P
description binding site for residue GOL B 305
source : AD6
12) chain B
residue 201
type
sequence P
description binding site for residue GOL B 305
source : AD6
13) chain B
residue 17
type
sequence H
description binding site for residue ZN B 306
source : AD7
14) chain B
residue 72
type
sequence D
description binding site for residue ZN B 307
source : AD8
15) chain B
residue 75
type
sequence D
description binding site for residue ZN B 308
source : AD9
16) chain B
residue 89
type
sequence R
description binding site for residue ZN B 308
source : AD9
17) chain B
residue 35
type
sequence T
description binding site for residue GOL B 309
source : AE1
18) chain B
residue 38
type
sequence A
description binding site for residue GOL B 309
source : AE1
19) chain B
residue 191
type
sequence W
description binding site for residue GOL B 309
source : AE1
20) chain B
residue 259
type
sequence F
description binding site for residue GOL B 309
source : AE1
21) chain B
residue 62
type
sequence N
description binding site for residues QVS A 305 and QCL B 301
source : AE4
22) chain B
residue 199
type
sequence T
description binding site for residues QVS A 305 and QCL B 301
source : AE4
23) chain B
residue 200
type
sequence P
description binding site for residues QVS A 305 and QCL B 301
source : AE4
24) chain B
residue 201
type
sequence P
description binding site for residues QVS A 305 and QCL B 301
source : AE4
25) chain B
residue 4
type
sequence H
description binding site for residues QCL A 317 and QVS A 318
source : AE6
26) chain B
residue 4
type
sequence H
description binding site for residues QVS A 318 and QUK A 319
source : AE7
27) chain B
residue 19
type
sequence D
description binding site for residues QVS A 318 and QUK A 319
source : AE7
28) chain B
residue 20
type
sequence F
description binding site for residues QVS A 318 and QUK A 319
source : AE7
29) chain B
residue 4
type
sequence H
description binding site for residues QUK A 319 and QVE A 320
source : AE8
30) chain B
residue 5
type
sequence W
description binding site for residues QUK A 319 and QVE A 320
source : AE8
31) chain B
residue 19
type
sequence D
description binding site for residues QUK A 319 and QVE A 320
source : AE8
32) chain B
residue 20
type
sequence F
description binding site for residues QUK A 319 and QVE A 320
source : AE8
33) chain B
residue 64
type
sequence H
description binding site for residues QUK A 319 and QVE A 320
source : AE8
34) chain B
residue 94
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
35) chain B
residue 96
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
36) chain B
residue 119
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
37) chain B
residue 130
type
sequence F
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
38) chain B
residue 197
type
sequence L
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
39) chain B
residue 198
type
sequence T
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
40) chain B
residue 199
type
sequence T
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
41) chain B
residue 201
type
sequence P
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
42) chain B
residue 208
type
sequence W
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
43) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2
44) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2
45) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2
46) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2
47) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2
48) chain B
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA2
49) 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
50) 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
51) chain B
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
52) 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
53) chain B
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
54) chain B
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
55) 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
56) 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
57) 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
58) 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
59) 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

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