eF-site ID 1aui-AB
PDB Code 1aui
Chain A, B

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Title HUMAN CALCINEURIN HETERODIMER
Classification HYDROLASE
Compound SERINE/THREONINE PHOSPHATASE 2B
Source Homo sapiens (Human) (CANB1_HUMAN)
Sequence A:  TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKE
GRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHG
QFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYL
WALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSER
VYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTV
RGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRK
SQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQ
FNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICS
SFEEAKGLDRINERMPPR
B:  SYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMS
LPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVK
GDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLK
DTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKK
MVVDV
Description


Functional site

1) chain A
residue 90
type
sequence D
description FE BINDING SITE.
source : FEB

2) chain A
residue 92
type
sequence H
description FE BINDING SITE.
source : FEB

3) chain A
residue 118
type
sequence D
description FE BINDING SITE.
source : FEB

4) chain A
residue 118
type
sequence D
description ZN BINDING SITE.
source : ZNB

5) chain A
residue 150
type
sequence N
description ZN BINDING SITE.
source : ZNB

6) chain A
residue 199
type
sequence H
description ZN BINDING SITE.
source : ZNB

7) chain A
residue 281
type
sequence H
description ZN BINDING SITE.
source : ZNB

8) chain B
residue 30
type
sequence D
description CALCIUM BINDING SITE.
source : CA1

9) chain B
residue 32
type
sequence D
description CALCIUM BINDING SITE.
source : CA1

10) chain B
residue 34
type
sequence S
description CALCIUM BINDING SITE.
source : CA1

11) chain B
residue 36
type
sequence S
description CALCIUM BINDING SITE.
source : CA1

12) chain B
residue 41
type
sequence E
description CALCIUM BINDING SITE.
source : CA1

13) chain B
residue 62
type
sequence D
description CALCIUM BINDING SITE.
source : CA2

14) chain B
residue 64
type
sequence D
description CALCIUM BINDING SITE.
source : CA2

15) chain B
residue 66
type
sequence N
description CALCIUM BINDING SITE.
source : CA2

16) chain B
residue 68
type
sequence E
description CALCIUM BINDING SITE.
source : CA2

17) chain B
residue 73
type
sequence E
description CALCIUM BINDING SITE.
source : CA2

18) chain B
residue 99
type
sequence D
description CALCIUM BINDING SITE.
source : CA3

19) chain B
residue 101
type
sequence D
description CALCIUM BINDING SITE.
source : CA3

20) chain B
residue 103
type
sequence D
description CALCIUM BINDING SITE.
source : CA3

21) chain B
residue 105
type
sequence Y
description CALCIUM BINDING SITE.
source : CA3

22) chain B
residue 110
type
sequence E
description CALCIUM BINDING SITE.
source : CA3

23) chain B
residue 140
type
sequence D
description CALCIUM BINDING SITE.
source : CA4

24) chain B
residue 142
type
sequence D
description CALCIUM BINDING SITE.
source : CA4

25) chain B
residue 144
type
sequence D
description CALCIUM BINDING SITE.
source : CA4

26) chain B
residue 146
type
sequence R
description CALCIUM BINDING SITE.
source : CA4

27) chain B
residue 151
type
sequence E
description CALCIUM BINDING SITE.
source : CA4

28) chain B
residue 30
type
sequence D
description BINDING SITE FOR RESIDUE CA B 500
source : AC1

29) chain B
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE CA B 500
source : AC1

30) chain B
residue 34
type
sequence S
description BINDING SITE FOR RESIDUE CA B 500
source : AC1

31) chain B
residue 36
type
sequence S
description BINDING SITE FOR RESIDUE CA B 500
source : AC1

32) chain B
residue 41
type
sequence E
description BINDING SITE FOR RESIDUE CA B 500
source : AC1

33) chain B
residue 62
type
sequence D
description BINDING SITE FOR RESIDUE CA B 501
source : AC2

34) chain B
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE CA B 501
source : AC2

35) chain B
residue 66
type
sequence N
description BINDING SITE FOR RESIDUE CA B 501
source : AC2

36) chain B
residue 68
type
sequence E
description BINDING SITE FOR RESIDUE CA B 501
source : AC2

37) chain B
residue 73
type
sequence E
description BINDING SITE FOR RESIDUE CA B 501
source : AC2

38) chain B
residue 99
type
sequence D
description BINDING SITE FOR RESIDUE CA B 502
source : AC3

39) chain B
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE CA B 502
source : AC3

40) chain B
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA B 502
source : AC3

41) chain B
residue 105
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 502
source : AC3

42) chain B
residue 110
type
sequence E
description BINDING SITE FOR RESIDUE CA B 502
source : AC3

43) chain B
residue 140
type
sequence D
description BINDING SITE FOR RESIDUE CA B 503
source : AC4

44) chain B
residue 142
type
sequence D
description BINDING SITE FOR RESIDUE CA B 503
source : AC4

45) chain B
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE CA B 503
source : AC4

46) chain B
residue 146
type
sequence R
description BINDING SITE FOR RESIDUE CA B 503
source : AC4

47) chain B
residue 151
type
sequence E
description BINDING SITE FOR RESIDUE CA B 503
source : AC4

48) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 522
source : AC5

49) chain A
residue 150
type
sequence N
description BINDING SITE FOR RESIDUE ZN A 522
source : AC5

50) chain A
residue 199
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 522
source : AC5

51) chain A
residue 281
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 522
source : AC5

52) chain A
residue 90
type
sequence D
description BINDING SITE FOR RESIDUE FE A 523
source : AC6

53) chain A
residue 92
type
sequence H
description BINDING SITE FOR RESIDUE FE A 523
source : AC6

54) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE FE A 523
source : AC6

55) chain A
residue 469
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P63329
source Swiss-Prot : SWS_FT_FI6

56) chain A
residue 90
type catalytic
sequence D
description 406
source MCSA : MCSA1

57) chain A
residue 281
type catalytic
sequence H
description 406
source MCSA : MCSA1

58) chain A
residue 92
type catalytic
sequence H
description 406
source MCSA : MCSA1

59) chain A
residue 118
type catalytic
sequence D
description 406
source MCSA : MCSA1

60) chain A
residue 121
type catalytic
sequence D
description 406
source MCSA : MCSA1

61) chain A
residue 122
type catalytic
sequence R
description 406
source MCSA : MCSA1

62) chain A
residue 150
type catalytic
sequence N
description 406
source MCSA : MCSA1

63) chain A
residue 151
type catalytic
sequence H
description 406
source MCSA : MCSA1

64) chain A
residue 199
type catalytic
sequence H
description 406
source MCSA : MCSA1

65) chain A
residue 254
type catalytic
sequence R
description 406
source MCSA : MCSA1

66) chain B
residue 30-42
type prosite
sequence DLDNSGSLSVEEF
description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
source prosite : PS00018

67) chain B
residue 62-74
type prosite
sequence DTDGNGEVDFKEF
description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
source prosite : PS00018

68) chain B
residue 99-111
type prosite
sequence DMDKDGYISNGEL
description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
source prosite : PS00018

69) chain B
residue 140-152
type prosite
sequence DKDGDGRISFEEF
description EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
source prosite : PS00018

70) chain B
residue 31
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

71) chain B
residue 74
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

72) chain B
residue 141
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

73) chain B
residue 143
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

74) chain B
residue 145
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

75) chain B
residue 147
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

76) chain B
residue 152
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

77) chain B
residue 33
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

78) chain B
residue 35
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

79) chain B
residue 37
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

80) chain B
residue 42
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

81) chain B
residue 63
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

82) chain B
residue 65
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

83) chain B
residue 67
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

84) chain B
residue 69
type BINDING
sequence V
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI1

85) chain B
residue 100
type BINDING
sequence M
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

86) chain B
residue 102
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

87) chain B
residue 104
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

88) chain B
residue 106
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

89) chain B
residue 111
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

90) chain A
residue 281
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
source Swiss-Prot : SWS_FT_FI2

91) chain B
residue 118
type SITE
sequence M
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000269|PubMed:23468591
source Swiss-Prot : SWS_FT_FI3

92) chain B
residue 122
type SITE
sequence N
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000269|PubMed:23468591
source Swiss-Prot : SWS_FT_FI3

93) chain B
residue 106
type MOD_RES
sequence I
description Phosphotyrosine => ECO:0000250|UniProtKB:Q63810
source Swiss-Prot : SWS_FT_FI4

94) chain A
residue 147-152
type prosite
sequence LRGNHE
description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
source prosite : PS00125


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