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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