eF-site ID 5l6t-AB
PDB Code 5l6t
Chain A, 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 (5L6T)
Sequence A:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
B:  HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSQVLKFRKLNFNGEELMVDNWRPAQ
PLKNRQIKASF
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 302
source : AC2
5) chain A
residue 64
type
sequence H
description binding site for residue ZN A 302
source : AC2
6) chain A
residue 62
type
sequence N
description binding site for residue GOL A 303
source : AC3
7) chain A
residue 64
type
sequence H
description binding site for residue GOL A 303
source : AC3
8) chain A
residue 199
type
sequence T
description binding site for residue GOL A 303
source : AC3
9) chain A
residue 200
type
sequence P
description binding site for residue GOL A 303
source : AC3
10) chain A
residue 17
type
sequence H
description binding site for residue ZN A 304
source : AC4
11) chain A
residue 36
type
sequence H
description binding site for residue ZN A 305
source : AC5
12) chain B
residue 34
type
sequence D
description binding site for residue ZN A 305
source : AC5
13) chain A
residue 34
type
sequence D
description binding site for residue ZN A 306
source : AC6
14) chain B
residue 36
type
sequence H
description binding site for residue ZN A 306
source : AC6
15) chain A
residue 174
type
sequence D
description binding site for residue ZN A 307
source : AC7
16) chain A
residue 238
type
sequence E
description binding site for residue ZN A 308
source : AC8
17) chain A
residue 72
type
sequence D
description binding site for residue ZN A 310
source : AD1
18) chain A
residue 171
type
sequence K
description binding site for residue ZN A 311
source : AD2
19) chain A
residue 233
type
sequence E
description binding site for residue ZN A 311
source : AD2
20) chain B
residue 174
type
sequence D
description binding site for residue ZN A 311
source : AD2
21) chain A
residue 35
type
sequence T
description binding site for residue GOL A 312
source : AD3
22) chain A
residue 38
type
sequence A
description binding site for residue GOL A 312
source : AD3
23) chain A
residue 191
type
sequence W
description binding site for residue GOL A 312
source : AD3
24) chain A
residue 259
type
sequence F
description binding site for residue GOL A 312
source : AD3
25) chain A
residue 260
type
sequence K
description binding site for residue GOL A 312
source : AD3
26) chain B
residue 94
type
sequence H
description binding site for residue ZN B 301
source : AD4
27) chain B
residue 96
type
sequence H
description binding site for residue ZN B 301
source : AD4
28) chain B
residue 119
type
sequence H
description binding site for residue ZN B 301
source : AD4
29) chain B
residue 4
type
sequence H
description binding site for residue ZN B 302
source : AD5
30) chain B
residue 64
type
sequence H
description binding site for residue ZN B 302
source : AD5
31) chain B
residue 62
type
sequence N
description binding site for residue GOL B 303
source : AD6
32) chain B
residue 199
type
sequence T
description binding site for residue GOL B 303
source : AD6
33) chain B
residue 200
type
sequence P
description binding site for residue GOL B 303
source : AD6
34) chain B
residue 201
type
sequence P
description binding site for residue GOL B 303
source : AD6
35) chain B
residue 17
type
sequence H
description binding site for residue ZN B 304
source : AD7
36) chain B
residue 72
type
sequence D
description binding site for residue ZN B 305
source : AD8
37) chain B
residue 75
type
sequence D
description binding site for residue ZN B 306
source : AD9
38) chain B
residue 89
type
sequence R
description binding site for residue ZN B 306
source : AD9
39) chain B
residue 35
type
sequence T
description binding site for residue GOL B 307
source : AE1
40) chain B
residue 38
type
sequence A
description binding site for residue GOL B 307
source : AE1
41) chain B
residue 191
type
sequence W
description binding site for residue GOL B 307
source : AE1
42) chain B
residue 259
type
sequence F
description binding site for residue GOL B 307
source : AE1
43) chain A
residue 4
type
sequence H
description binding site for residues QVS A 305 and QUK A 306
source : AE3
44) chain A
residue 19
type
sequence D
description binding site for residues QVS A 305 and QUK A 306
source : AE3
45) chain A
residue 20
type
sequence F
description binding site for residues QVS A 305 and QUK A 306
source : AE3
46) chain A
residue 4
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
47) chain A
residue 94
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
48) chain A
residue 96
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
49) chain A
residue 119
type
sequence H
description binding site for residues QVS A 305 and QCL B 301
source : AE4
50) chain B
residue 62
type
sequence N
description binding site for residues QVS A 305 and QCL B 301
source : AE4
51) chain B
residue 199
type
sequence T
description binding site for residues QVS A 305 and QCL B 301
source : AE4
52) chain B
residue 200
type
sequence P
description binding site for residues QVS A 305 and QCL B 301
source : AE4
53) chain B
residue 201
type
sequence P
description binding site for residues QVS A 305 and QCL B 301
source : AE4
54) chain A
residue 4
type
sequence H
description binding site for residues QUK A 306 and QVE A 307
source : AE5
55) chain A
residue 5
type
sequence W
description binding site for residues QUK A 306 and QVE A 307
source : AE5
56) chain A
residue 19
type
sequence D
description binding site for residues QUK A 306 and QVE A 307
source : AE5
57) chain A
residue 20
type
sequence F
description binding site for residues QUK A 306 and QVE A 307
source : AE5
58) chain A
residue 64
type
sequence H
description binding site for residues QUK A 306 and QVE A 307
source : AE5
59) chain B
residue 4
type
sequence H
description binding site for residues QCL A 317 and QVS A 318
source : AE6
60) chain B
residue 4
type
sequence H
description binding site for residues QVS A 318 and QUK A 319
source : AE7
61) chain B
residue 19
type
sequence D
description binding site for residues QVS A 318 and QUK A 319
source : AE7
62) chain B
residue 20
type
sequence F
description binding site for residues QVS A 318 and QUK A 319
source : AE7
63) chain B
residue 4
type
sequence H
description binding site for residues QUK A 319 and QVE A 320
source : AE8
64) chain B
residue 5
type
sequence W
description binding site for residues QUK A 319 and QVE A 320
source : AE8
65) chain B
residue 19
type
sequence D
description binding site for residues QUK A 319 and QVE A 320
source : AE8
66) chain B
residue 20
type
sequence F
description binding site for residues QUK A 319 and QVE A 320
source : AE8
67) chain B
residue 64
type
sequence H
description binding site for residues QUK A 319 and QVE A 320
source : AE8
68) chain B
residue 94
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
69) chain B
residue 96
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
70) chain B
residue 119
type
sequence H
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
71) chain B
residue 130
type
sequence F
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
72) chain B
residue 197
type
sequence L
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
73) chain B
residue 198
type
sequence T
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
74) chain B
residue 199
type
sequence T
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
75) chain B
residue 201
type
sequence P
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
76) chain B
residue 208
type
sequence W
description binding site for residues QCL B 301 and 6H0 B 303
source : AE9
77) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1
78) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1
79) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1
80) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1
81) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1
82) chain A
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA1
83) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2
84) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2
85) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2
86) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2
87) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2
88) chain B
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA2
89) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
90) 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
91) 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
92) 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
93) 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
94) 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
95) 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
96) 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
97) 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
98) chain A
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
99) chain B
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
100) 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
101) 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
102) 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
103) 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
104) 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
105) 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
106) 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
107) 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
108) chain A
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
109) chain A
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
110) chain B
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
111) chain B
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

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