eF-site ID 2lqp_2-A
PDB Code 2lqp
Model 2
Chain A

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Title NMR solution structure of the Ca2+-Calmodulin C-terminal domain in a complex with a peptide (NSCaTE) from the L-type Voltage-Gated Calcium Channel alpha1C subunit
Classification METAL BINDING PROTEIN
Compound Calmodulin
Source Homo sapiens (Human) (CALM_HUMAN)
Sequence A:  DTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLT
DEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Description


Functional site

1) chain A
residue 93
type
sequence D
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

2) chain A
residue 97
type
sequence N
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

3) chain A
residue 99
type
sequence Y
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

4) chain A
residue 100
type
sequence I
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

5) chain A
residue 101
type
sequence S
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

6) chain A
residue 104
type
sequence E
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

7) chain A
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA A 201
source : AC1

8) chain A
residue 129
type
sequence D
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

9) chain A
residue 130
type
sequence I
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

10) chain A
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

11) chain A
residue 133
type
sequence D
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

12) chain A
residue 135
type
sequence Q
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

13) chain A
residue 140
type
sequence E
description BINDING SITE FOR RESIDUE CA A 202
source : AC2

14) chain A
residue 93
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

15) chain A
residue 140
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

16) chain A
residue 95
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

17) chain A
residue 97
type BINDING
sequence N
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

18) chain A
residue 99
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

19) chain A
residue 104
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 129
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 131
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 133
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

23) chain A
residue 135
type BINDING
sequence Q
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585
source Swiss-Prot : SWS_FT_FI1

24) chain A
residue 81
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI2

25) chain A
residue 94
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI3

26) chain A
residue 99
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI4

27) chain A
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_FI5

28) chain A
residue 110
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

29) chain A
residue 138
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8

30) chain A
residue 115
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI7

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

32) 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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