eF-site ID 1lvc-E
PDB Code 1lvc
Chain E

click to enlarge
Title Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP
Classification LYASE
Compound calmodulin-sensitive adenylate cyclase
Source (CALM_HUMAN)
Sequence E:  TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPT
EAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEE
IREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEM
IREADIDGDGQVNYEEFVQMMTA
Description


Functional site

1) chain E
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE CA E 802
source : AC3

2) chain E
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE CA E 802
source : AC3

3) chain E
residue 133
type
sequence D
description BINDING SITE FOR RESIDUE CA E 802
source : AC3

4) chain E
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA E 802
source : AC3

5) chain E
residue 140
type
sequence E
description BINDING SITE FOR RESIDUE CA E 802
source : AC3

6) chain E
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CA E 803
source : AC4

7) chain E
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE CA E 803
source : AC4

8) chain E
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE CA E 803
source : AC4

9) chain E
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE CA E 803
source : AC4

10) chain E
residue 104
type
sequence E
description BINDING SITE FOR RESIDUE CA E 803
source : AC4

11) chain E
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_FI10

12) chain E
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

13) chain E
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

14) chain E
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

15) chain E
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

16) chain E
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

17) chain E
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

18) chain E
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

19) chain E
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

20) chain E
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

21) chain E
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

22) chain E
residue 110
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI11

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

24) chain E
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

25) chain E
residue 44
type MOD_RES
sequence T
description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
source Swiss-Prot : SWS_FT_FI6

26) chain E
residue 115
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI4

27) chain E
residue 21
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI5

28) chain E
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

29) chain E
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

30) chain E
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

31) chain E
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

32) chain E
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

33) chain E
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

34) chain E
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

35) chain E
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

36) chain E
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

37) chain E
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

38) chain E
residue 81
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI7

39) chain E
residue 94
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI8

40) chain E
residue 99
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI9


Display surface

Download
Links