eF-site ID 1aui-B
PDB Code 1aui
Chain B

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Title HUMAN CALCINEURIN HETERODIMER
Classification HYDROLASE
Compound SERINE/THREONINE PHOSPHATASE 2B
Source null (CANB1_HUMAN)
Sequence B:  SYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMS
LPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVK
GDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLK
DTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKK
MVVDV
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

45) 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

46) 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

47) 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

48) 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

49) 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

50) 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

51) 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

52) 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

53) 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

54) 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

55) 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

56) 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

57) 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

58) 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

59) 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

60) 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

61) 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

62) 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

63) 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

64) 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

65) 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

66) 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

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


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