eF-site ID 4byf-B
PDB Code 4byf
Chain B

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Title Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state
Classification HYDROLASE
Compound UNCONVENTIONAL MYOSIN-IC
Source Homo sapiens (Human) (CALM_HUMAN)
Sequence B:  MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSL
GQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDT
DSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTA
Description


Functional site
1) chain B
residue 82
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6
2) chain B
residue 111
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10
3) chain B
residue 116
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
source Swiss-Prot : SWS_FT_FI11
4) chain B
residue 139
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI12
5) chain B
residue 21-33
type prosite
sequence DKDGDGTITTKEL
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
6) chain B
residue 57-69
type prosite
sequence DADGNGTIDFPEF
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
7) chain B
residue 94-106
type prosite
sequence DKDGNGYISAAEL
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
8) chain B
residue 130-142
type prosite
sequence DIDGDGQVNYEEF
description EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
source prosite : PS00018
9) chain B
residue 21
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
10) chain B
residue 23
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
11) chain B
residue 25
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
12) chain B
residue 27
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
13) chain B
residue 32
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
14) chain B
residue 68
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
15) chain B
residue 57
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 B
residue 59
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 B
residue 61
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
18) chain B
residue 63
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 B
residue 2
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3
20) chain B
residue 45
type MOD_RES
sequence T
description Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
source Swiss-Prot : SWS_FT_FI5
21) chain B
residue 94
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
22) chain B
residue 96
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
23) chain B
residue 98
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
24) chain B
residue 100
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
25) chain B
residue 141
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
26) chain B
residue 105
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
27) chain B
residue 130
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
28) chain B
residue 132
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 B
residue 134
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 B
residue 136
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
31) chain B
residue 22
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI4
32) chain B
residue 22
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
33) chain B
residue 95
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7
34) chain B
residue 100
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8
35) chain B
residue 102
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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