eF-site ID 5l70-B
PDB Code 5l70
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 (5L70)
Sequence B:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
Description


Functional site

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

2) chain B
residue 36
type
sequence H
description binding site for residue ZN A 306
source : AC6

3) chain B
residue 233
type
sequence E
description binding site for residue ZN A 307
source : AC7

4) chain B
residue 94
type
sequence H
description binding site for residue ZN B 301
source : AD3

5) chain B
residue 96
type
sequence H
description binding site for residue ZN B 301
source : AD3

6) chain B
residue 119
type
sequence H
description binding site for residue ZN B 301
source : AD3

7) chain B
residue 4
type
sequence H
description binding site for residue ZN B 302
source : AD4

8) chain B
residue 64
type
sequence H
description binding site for residue ZN B 302
source : AD4

9) chain B
residue 5
type
sequence W
description binding site for residue GOL B 303
source : AD5

10) chain B
residue 62
type
sequence N
description binding site for residue GOL B 303
source : AD5

11) chain B
residue 199
type
sequence T
description binding site for residue GOL B 303
source : AD5

12) chain B
residue 200
type
sequence P
description binding site for residue GOL B 303
source : AD5

13) chain B
residue 201
type
sequence P
description binding site for residue GOL B 303
source : AD5

14) chain B
residue 17
type
sequence H
description binding site for residue ZN B 304
source : AD6

15) chain B
residue 72
type
sequence D
description binding site for residue ZN B 305
source : AD7

16) chain B
residue 35
type
sequence T
description binding site for residue GOL B 306
source : AD8

17) chain B
residue 38
type
sequence A
description binding site for residue GOL B 306
source : AD8

18) chain B
residue 191
type
sequence W
description binding site for residue GOL B 306
source : AD8

19) chain B
residue 259
type
sequence F
description binding site for residue GOL B 306
source : AD8

20) chain B
residue 260
type
sequence K
description binding site for residue GOL B 306
source : AD8

21) chain B
residue 5
type
sequence W
description binding site for residues QVS A 305 and QOL B 301
source : AE2

22) chain B
residue 62
type
sequence N
description binding site for residues QVS A 305 and QOL B 301
source : AE2

23) chain B
residue 199
type
sequence T
description binding site for residues QVS A 305 and QOL B 301
source : AE2

24) chain B
residue 200
type
sequence P
description binding site for residues QVS A 305 and QOL B 301
source : AE2

25) chain B
residue 201
type
sequence P
description binding site for residues QVS A 305 and QOL B 301
source : AE2

26) chain B
residue 4
type
sequence H
description binding site for residues QOL A 316 and QVS A 317
source : AE4

27) chain B
residue 4
type
sequence H
description binding site for residues QVS A 317 and QUK A 318
source : AE5

28) chain B
residue 19
type
sequence D
description binding site for residues QVS A 317 and QUK A 318
source : AE5

29) chain B
residue 20
type
sequence F
description binding site for residues QVS A 317 and QUK A 318
source : AE5

30) chain B
residue 4
type
sequence H
description binding site for residues QUK A 318 and QVE A 319
source : AE6

31) chain B
residue 5
type
sequence W
description binding site for residues QUK A 318 and QVE A 319
source : AE6

32) chain B
residue 19
type
sequence D
description binding site for residues QUK A 318 and QVE A 319
source : AE6

33) chain B
residue 20
type
sequence F
description binding site for residues QUK A 318 and QVE A 319
source : AE6

34) chain B
residue 64
type
sequence H
description binding site for residues QUK A 318 and QVE A 319
source : AE6

35) chain B
residue 94
type
sequence H
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

36) chain B
residue 96
type
sequence H
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

37) chain B
residue 119
type
sequence H
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

38) chain B
residue 121
type
sequence V
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

39) chain B
residue 130
type
sequence F
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

40) chain B
residue 142
type
sequence V
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

41) chain B
residue 197
type
sequence L
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

42) chain B
residue 198
type
sequence T
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

43) chain B
residue 199
type
sequence T
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

44) chain B
residue 201
type
sequence P
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

45) chain B
residue 208
type
sequence W
description binding site for residues QOL B 301 and 6H0 B 303
source : AE7

46) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2

47) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2

48) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2

49) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2

50) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2

51) chain B
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA2

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 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

54) 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

55) 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

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

57) 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

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

60) 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

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

62) 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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