eF-site ID 4orb-AB
PDB Code 4orb
Chain A, B

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Title Crystal structure of mouse calcineurin
Classification HYDROLASE/METAL BINDING PROTEIN
Compound Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
Source Mus musculus (Mouse) (CANB1_MOUSE)
Sequence A:  TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKE
GRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHG
QFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYL
WALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSER
VYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR
KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTV
RGCSYFYSYPAVCDFLQHNNLLSILRAHEAQDAGYRMYRK
SQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQ
FNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICS
SFEEAKGLDRINERMPP
B:  SYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMS
LPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVK
GDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLK
DTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKK
MVVDV
Description


Functional site

1) chain A
residue 90
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 601
source : AC1

2) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 601
source : AC1

3) chain A
residue 150
type
sequence N
description BINDING SITE FOR RESIDUE ZN A 601
source : AC1

4) chain A
residue 199
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 601
source : AC1

5) chain A
residue 281
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 601
source : AC1

6) chain A
residue 90
type
sequence D
description BINDING SITE FOR RESIDUE FE A 602
source : AC2

7) chain A
residue 92
type
sequence H
description BINDING SITE FOR RESIDUE FE A 602
source : AC2

8) chain A
residue 118
type
sequence D
description BINDING SITE FOR RESIDUE FE A 602
source : AC2

9) chain B
residue 62
type
sequence D
description BINDING SITE FOR RESIDUE CA B 201
source : AC3

10) chain B
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE CA B 201
source : AC3

11) chain B
residue 66
type
sequence N
description BINDING SITE FOR RESIDUE CA B 201
source : AC3

12) chain B
residue 68
type
sequence E
description BINDING SITE FOR RESIDUE CA B 201
source : AC3

13) chain B
residue 73
type
sequence E
description BINDING SITE FOR RESIDUE CA B 201
source : AC3

14) chain B
residue 99
type
sequence D
description BINDING SITE FOR RESIDUE CA B 202
source : AC4

15) chain B
residue 101
type
sequence D
description BINDING SITE FOR RESIDUE CA B 202
source : AC4

16) chain B
residue 103
type
sequence D
description BINDING SITE FOR RESIDUE CA B 202
source : AC4

17) chain B
residue 105
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 202
source : AC4

18) chain B
residue 110
type
sequence E
description BINDING SITE FOR RESIDUE CA B 202
source : AC4

19) chain B
residue 140
type
sequence D
description BINDING SITE FOR RESIDUE CA B 203
source : AC5

20) chain B
residue 142
type
sequence D
description BINDING SITE FOR RESIDUE CA B 203
source : AC5

21) chain B
residue 144
type
sequence D
description BINDING SITE FOR RESIDUE CA B 203
source : AC5

22) chain B
residue 146
type
sequence R
description BINDING SITE FOR RESIDUE CA B 203
source : AC5

23) chain B
residue 151
type
sequence E
description BINDING SITE FOR RESIDUE CA B 203
source : AC5

24) chain B
residue 30
type
sequence D
description BINDING SITE FOR RESIDUE CA B 204
source : AC6

25) chain B
residue 32
type
sequence D
description BINDING SITE FOR RESIDUE CA B 204
source : AC6

26) chain B
residue 34
type
sequence S
description BINDING SITE FOR RESIDUE CA B 204
source : AC6

27) chain B
residue 36
type
sequence S
description BINDING SITE FOR RESIDUE CA B 204
source : AC6

28) chain B
residue 41
type
sequence E
description BINDING SITE FOR RESIDUE CA B 204
source : AC6

29) chain B
residue 30
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 73
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 99
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 101
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 103
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 105
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 110
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

36) chain B
residue 140
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

37) chain B
residue 142
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

38) chain B
residue 144
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

39) chain B
residue 146
type BINDING
sequence R
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

40) chain B
residue 32
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 151
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

42) chain B
residue 34
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

43) chain B
residue 36
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

44) chain B
residue 41
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

45) chain B
residue 62
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

46) chain B
residue 64
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 66
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

48) chain B
residue 68
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:26794871, ECO:0007744|PDB:4ORB
source Swiss-Prot : SWS_FT_FI1

49) chain B
residue 117
type SITE
sequence M
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

50) chain B
residue 121
type SITE
sequence N
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 118
type SITE
sequence D
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 150
type SITE
sequence N
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 199
type SITE
sequence H
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 281
type SITE
sequence H
description Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000250|UniProtKB:P63098
source Swiss-Prot : SWS_FT_FI2

55) chain B
residue 105
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18034455
source Swiss-Prot : SWS_FT_FI3

56) chain A
residue 224
type MOD_RES
sequence Y
description 3'-nitrotyrosine => ECO:0007744|PubMed:16800626
source Swiss-Prot : SWS_FT_FI5

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

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

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

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

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

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


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