eF-site ID 5l9e-A
PDB Code 5l9e
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 (5L9E)
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 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 17
type
sequence H
description binding site for residue ZN A 303
source : AC3

7) chain A
residue 174
type
sequence D
description binding site for residue ZN A 304
source : AC4

8) chain A
residue 34
type
sequence D
description binding site for residue ZN A 305
source : AC5

9) chain A
residue 36
type
sequence H
description binding site for residue ZN A 305
source : AC5

10) chain A
residue 186
type
sequence E
description binding site for residue ZN A 306
source : AC6

11) chain A
residue 52
type
sequence D
description binding site for residue ZN A 307
source : AC7

12) chain A
residue 15
type
sequence H
description binding site for residue ZN A 308
source : AC8

13) chain A
residue 62
type
sequence N
description binding site for residue GOL A 309
source : AC9

14) chain A
residue 65
type
sequence A
description binding site for residue GOL A 309
source : AC9

15) chain A
residue 67
type
sequence N
description binding site for residue GOL A 309
source : AC9

16) chain A
residue 92
type
sequence Q
description binding site for residue GOL A 309
source : AC9

17) chain A
residue 189
type
sequence D
description binding site for residue ZN A 310
source : AD1

18) chain A
residue 260
type
sequence K
description binding site for residue ZN A 310
source : AD1

19) chain A
residue 233
type
sequence E
description binding site for residue ZN A 311
source : AD2

20) chain A
residue 233
type
sequence E
description binding site for residue ZN A 311
source : AD2

21) chain A
residue 26
type
sequence E
description binding site for residue ZN C 303
source : AE2

22) chain A
residue 4
type
sequence H
description binding site for residues QUJ A 303 and QVE A 304
source : AF6

23) chain A
residue 169
type
sequence K
description binding site for residues QUJ A 303 and QVE A 304
source : AF6

24) chain A
residue 4
type
sequence H
description binding site for residues QVE A 304 and QUJ A 305
source : AF7

25) chain A
residue 19
type
sequence D
description binding site for residues QVE A 304 and QUJ A 305
source : AF7

26) chain A
residue 20
type
sequence F
description binding site for residues QVE A 304 and QUJ A 305
source : AF7

27) chain A
residue 169
type
sequence K
description binding site for residues QVE A 304 and QUJ A 305
source : AF7

28) chain A
residue 201
type
sequence P
description binding site for residues QVE A 304 and QUJ A 305
source : AF7

29) chain A
residue 4
type
sequence H
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

30) chain A
residue 5
type
sequence W
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

31) chain A
residue 19
type
sequence D
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

32) chain A
residue 20
type
sequence F
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

33) chain A
residue 64
type
sequence H
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

34) chain A
residue 201
type
sequence P
description binding site for residues QUJ A 305 and QVE A 306
source : AF8

35) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1

36) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1

37) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1

38) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1

39) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1

40) chain A
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA1

41) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162

42) 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

43) 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

44) 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

45) 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

46) chain A
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4

47) 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

48) 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

49) 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

50) 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

51) chain A
residue 2
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P27139
source Swiss-Prot : SWS_FT_FI8

52) chain A
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

53) 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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