eF-site ID 5l6k-A
PDB Code 5l6k
Chain A

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Title Crystal Structure of Human Carbonic Anhydrase II in Complex with a Quinoline Oligoamide Foldamer
Classification LYASE
Compound Carbonic anhydrase 2
Source (5L6K)
Sequence A:  SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYD
PSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV
HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPP
LLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
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 62
type
sequence N
description binding site for residue GOL A 302
source : AC2
5) chain A
residue 65
type
sequence A
description binding site for residue GOL A 302
source : AC2
6) chain A
residue 67
type
sequence N
description binding site for residue GOL A 302
source : AC2
7) chain A
residue 92
type
sequence Q
description binding site for residue GOL A 302
source : AC2
8) chain A
residue 94
type
sequence H
description binding site for residue GOL A 302
source : AC2
9) chain A
residue 199
type
sequence T
description binding site for residue GOL A 302
source : AC2
10) chain A
residue 67
type
sequence N
description binding site for residue GOL A 303
source : AC3
11) chain A
residue 69
type
sequence E
description binding site for residue GOL A 303
source : AC3
12) chain A
residue 92
type
sequence Q
description binding site for residue GOL A 303
source : AC3
13) chain A
residue 130
type
sequence F
description binding site for residue GOL A 303
source : AC3
14) chain A
residue 32
type
sequence D
description binding site for residue NA A 304
source : AC7
15) chain A
residue 110
type
sequence D
description binding site for residue NA A 304
source : AC7
16) chain A
residue 11
type
sequence N
description binding site for residue DMS A 305
source : AC8
17) chain A
residue 15
type
sequence H
description binding site for residue DMS A 305
source : AC8
18) chain A
residue 16
type
sequence W
description binding site for residue DMS A 305
source : AC8
19) chain A
residue 18
type
sequence K
description binding site for residue DMS A 305
source : AC8
20) chain A
residue 19
type
sequence D
description binding site for residue DMS A 305
source : AC8
21) chain A
residue 3
type
sequence H
description binding site for residues QUK A 303 and QVS A 304
source : AD6
22) chain A
residue 19
type
sequence D
description binding site for residues QUK A 303 and QVS A 304
source : AD6
23) chain A
residue 20
type
sequence F
description binding site for residues QUK A 303 and QVS A 304
source : AD6
24) chain A
residue 3
type
sequence H
description binding site for residues QUK A 303 and QUJ A 315
source : AD7
25) chain A
residue 2
type
sequence S
description binding site for residues QVS A 304 and QVE A 305
source : AD8
26) chain A
residue 3
type
sequence H
description binding site for residues QVS A 304 and QVE A 305
source : AD8
27) chain A
residue 19
type
sequence D
description binding site for residues QVS A 304 and QVE A 305
source : AD8
28) chain A
residue 20
type
sequence F
description binding site for residues QVS A 304 and QVE A 305
source : AD8
29) chain A
residue 130
type
sequence F
description binding site for residues QUJ B 301 and 6H0 B 306
source : AE3
30) chain A
residue 131
type
sequence G
description binding site for residues QUJ B 301 and 6H0 B 306
source : AE3
31) chain A
residue 130
type
sequence F
description binding site for residues QUJ B 301 and QUK B 307
source : AE4
32) chain A
residue 131
type
sequence G
description binding site for residues QUJ B 301 and QUK B 307
source : AE4
33) chain A
residue 129
type
sequence D
description binding site for residues QUK B 307 and QVS B 308
source : AE6
34) chain A
residue 132
type
sequence K
description binding site for residues QUK B 307 and QVS B 308
source : AE6
35) chain A
residue 129
type
sequence D
description binding site for residues QVS B 308 and QVE B 309
source : AE7
36) chain A
residue 132
type
sequence K
description binding site for residues QVS B 308 and QVE B 309
source : AE7
37) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1
38) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1
39) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1
40) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1
41) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1
42) chain A
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA1
43) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162
44) 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
45) 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
46) 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
47) 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
48) chain A
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
49) 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
50) 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
51) 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
52) 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
53) chain A
residue 2
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P27139
source Swiss-Prot : SWS_FT_FI8
54) chain A
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9
55) chain A
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

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