eF-site ID 2col-B
PDB Code 2col
Chain B

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Title Crystal structure analysis of CyaA/C-Cam with Pyrophosphate
Classification LYASE/METAL BINDING PROTEIN
Compound Bifunctional hemolysin-adenylate cyclase
Source Bordetella pertussis (CALM_XENLA)
Sequence B:  TDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTD
EEVDEMIREADIDGDGQVNYEEFVQMM
Description


Functional site

1) chain B
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE CA B 800
source : AC1

2) chain B
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE CA B 800
source : AC1

3) chain B
residue 133
type
sequence D
description BINDING SITE FOR RESIDUE CA B 800
source : AC1

4) chain B
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA B 800
source : AC1

5) chain B
residue 140
type
sequence E
description BINDING SITE FOR RESIDUE CA B 800
source : AC1

6) chain B
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CA B 801
source : AC2

7) chain B
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE CA B 801
source : AC2

8) chain B
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE CA B 801
source : AC2

9) chain B
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE CA B 801
source : AC2

10) chain B
residue 104
type
sequence E
description BINDING SITE FOR RESIDUE CA B 801
source : AC2

11) chain B
residue 93-105
type prosite
sequence DKDGNGYISAAEL
description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL
source prosite : PS00018

12) chain B
residue 129-141
type prosite
sequence DIDGDGQVNYEEF
description EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYISaaEL
source prosite : PS00018

13) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

14) chain B
residue 141
type BINDING
sequence F
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

15) chain B
residue 96
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

16) chain B
residue 98
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

17) chain B
residue 100
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

18) chain B
residue 105
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

19) chain B
residue 130
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

20) chain B
residue 132
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

21) chain B
residue 134
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

22) chain B
residue 136
type BINDING
sequence V
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 116
type MOD_RES
sequence L
description N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P0DP23
source Swiss-Prot : SWS_FT_FI2


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