eF-site ID 1xfu-Q
PDB Code 1xfu
Chain Q

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Title Crystal structure of anthrax edema factor (EF) truncation mutant, EF-delta 64 in complex with calmodulin
Classification LYASE/Metal binding protein
Compound Calmodulin-sensitive adenylate cyclase
Source Bacillus anthracis (CALM_HUMAN)
Sequence Q:  QLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQN
PTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSE
EEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVD
QMIREADIDGDGQVNYEEFVQMMTAK
Description


Functional site

1) chain Q
residue 20
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 705
source : BC4

2) chain Q
residue 22
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 705
source : BC4

3) chain Q
residue 24
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 705
source : BC4

4) chain Q
residue 26
type
sequence T
description BINDING SITE FOR RESIDUE CA Q 705
source : BC4

5) chain Q
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 805
source : BC5

6) chain Q
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 805
source : BC5

7) chain Q
residue 133
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 805
source : BC5

8) chain Q
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA Q 805
source : BC5

9) chain Q
residue 140
type
sequence E
description BINDING SITE FOR RESIDUE CA Q 805
source : BC5

10) chain Q
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 806
source : BC6

11) chain Q
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE CA Q 806
source : BC6

12) chain Q
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE CA Q 806
source : BC6

13) chain Q
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE CA Q 806
source : BC6

14) chain Q
residue 104
type
sequence E
description BINDING SITE FOR RESIDUE CA Q 806
source : BC6

15) chain Q
residue 20
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

16) chain Q
residue 22
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

17) chain Q
residue 24
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

18) chain Q
residue 26
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

19) chain Q
residue 31
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

20) chain Q
residue 56
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

21) chain Q
residue 58
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

22) chain Q
residue 60
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

23) chain Q
residue 62
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

24) chain Q
residue 67
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI1

25) chain Q
residue 110
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10

26) chain Q
residue 115
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI11

27) chain Q
residue 138
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI12

28) chain Q
residue 21
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
source Swiss-Prot : SWS_FT_FI13

29) chain Q
residue 93
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

30) chain Q
residue 95
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

31) chain Q
residue 97
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

32) chain Q
residue 99
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

33) chain Q
residue 104
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

34) chain Q
residue 129
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

35) chain Q
residue 131
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

36) chain Q
residue 133
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

37) chain Q
residue 135
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

38) chain Q
residue 140
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
source Swiss-Prot : SWS_FT_FI2

39) chain Q
residue 21
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4

40) chain Q
residue 44
type MOD_RES
sequence T
description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
source Swiss-Prot : SWS_FT_FI5

41) chain Q
residue 81
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

42) chain Q
residue 94
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

43) chain Q
residue 99
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8

44) chain Q
residue 101
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


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