eF-site ID 2llq_3-AB
PDB Code 2llq
Model 3
Chain A, B

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Title Solution nmr-derived structure of calmodulin c-lobe bound with er alpha peptide
Classification METAL BINDING PROTEIN/HORMONE RECEPTOR
Compound Calmodulin
Source Xenopus laevis (African clawed frog) (ESR1_HUMAN)
Sequence A:  EEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMTAK
B:  RAANLWPSPLMIKRSKKNS
Description (1)  Calmodulin, Estrogen receptor


Functional site

1) chain A
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

2) chain A
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

3) chain A
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

4) chain A
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

5) chain A
residue 104
type
sequence E
description BINDING SITE FOR RESIDUE CA A 1000
source : AC1

6) chain A
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1001
source : AC2

7) chain A
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1001
source : AC2

8) chain A
residue 133
type
sequence D
description BINDING SITE FOR RESIDUE CA A 1001
source : AC2

9) chain A
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA A 1001
source : AC2

10) chain A
residue 140
type
sequence E
description BINDING SITE FOR RESIDUE CA A 1001
source : AC2

11) chain A
residue 93
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 140
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

13) chain A
residue 95
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 97
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 99
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 104
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 129
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 131
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 133
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 135
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 115
type MOD_RES
sequence K
description N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P0DP23
source Swiss-Prot : SWS_FT_FI2

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

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


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