Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BYF

Crystal structure of human Myosin 1c in complex with calmodulin in the pre-power stroke state

Functional Information from GO Data
ChainGOidnamespacecontents
A0003774molecular_functioncytoskeletal motor activity
A0005524molecular_functionATP binding
A0016459cellular_componentmyosin complex
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0002027biological_processregulation of heart rate
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0007186biological_processG protein-coupled receptor signaling pathway
B0008076cellular_componentvoltage-gated potassium channel complex
B0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
B0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0021762biological_processsubstantia nigra development
B0030017cellular_componentsarcomere
B0030234molecular_functionenzyme regulator activity
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031954biological_processpositive regulation of protein autophosphorylation
B0031982cellular_componentvesicle
B0032465biological_processregulation of cytokinesis
B0032516biological_processpositive regulation of phosphoprotein phosphatase activity
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0042995cellular_componentcell projection
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050848biological_processregulation of calcium-mediated signaling
B0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0071902biological_processpositive regulation of protein serine/threonine kinase activity
B0072542molecular_functionprotein phosphatase activator activity
B0097225cellular_componentsperm midpiece
B0098901biological_processregulation of cardiac muscle cell action potential
B0140056biological_processorganelle localization by membrane tethering
B1901842biological_processnegative regulation of high voltage-gated calcium channel activity
B1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
B1902494cellular_componentcatalytic complex
B1905913biological_processnegative regulation of calcium ion export across plasma membrane
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
C0003774molecular_functioncytoskeletal motor activity
C0005524molecular_functionATP binding
C0016459cellular_componentmyosin complex
D0000086biological_processG2/M transition of mitotic cell cycle
D0000922cellular_componentspindle pole
D0002027biological_processregulation of heart rate
D0005509molecular_functioncalcium ion binding
D0005513biological_processdetection of calcium ion
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0005929cellular_componentcilium
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
D0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
D0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
D0010856molecular_functionadenylate cyclase activator activity
D0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0016020cellular_componentmembrane
D0016240biological_processautophagosome membrane docking
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0030234molecular_functionenzyme regulator activity
D0031432molecular_functiontitin binding
D0031514cellular_componentmotile cilium
D0031954biological_processpositive regulation of protein autophosphorylation
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032516biological_processpositive regulation of phosphoprotein phosphatase activity
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0035307biological_processpositive regulation of protein dephosphorylation
D0035458biological_processcellular response to interferon-beta
D0042995cellular_componentcell projection
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044325molecular_functiontransmembrane transporter binding
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0050848biological_processregulation of calcium-mediated signaling
D0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
D0051592biological_processresponse to calcium ion
D0055117biological_processregulation of cardiac muscle contraction
D0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
D0071346biological_processcellular response to type II interferon
D0071902biological_processpositive regulation of protein serine/threonine kinase activity
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0098901biological_processregulation of cardiac muscle cell action potential
D0140056biological_processorganelle localization by membrane tethering
D1901842biological_processnegative regulation of high voltage-gated calcium channel activity
D1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
D1902494cellular_componentcatalytic complex
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
D1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 1000
ChainResidue
ATHR112
ASER161
AAOV1001
AHOH2010

site_idAC2
Number of Residues21
DetailsBINDING SITE FOR RESIDUE AOV A 1001
ChainResidue
AGLY108
AALA109
AGLY110
ALYS111
ATHR112
AGLU113
AASN157
AASN159
ASER160
ASER161
ATYR388
AGLY389
AMG1000
AHOH2010
AHOH2011
AHOH2056
AASN53
AARG56
ATYR61
AGLU106
ASER107

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 1000
ChainResidue
CTHR112
CSER161
CAOV1001
CHOH2019
CHOH2021

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE AOV C 1001
ChainResidue
CASN53
CARG56
CTYR61
CGLU106
CSER107
CGLY108
CALA109
CGLY110
CLYS111
CTHR112
CGLU113
CASN157
CASN159
CSER160
CSER161
CTYR388
CGLY389
CMG1000
CHOH2008
CHOH2019
CHOH2021
CHOH2055
CHOH2083

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 1000
ChainResidue
DASP94
DASP96
DASN98
DTYR100

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP21-LEU33
BASP57-PHE69
BASP94-LEU106
BASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: 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
ChainResidueDetails
BASP21
BGLU68
DASP21
DASP23
DASP25
DTHR27
DGLU32
DASP57
DASP59
DASN61
DTHR63
BASP23
DGLU68
BASP25
BTHR27
BGLU32
BASP57
BASP59
BASN61
BTHR63

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
BASP94
BGLU141
DASP94
DASP96
DASN98
DTYR100
DGLU105
DASP130
DASP132
DASP134
DGLN136
BASP96
DGLU141
BASN98
BTYR100
BGLU105
BASP130
BASP132
BASP134
BGLN136

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 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
ChainResidueDetails
BALA2
DALA2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS22
DLYS22

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
BTHR45
DTHR45

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER82
DSER82

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS95
DLYS95

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR100
DTYR100

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER102
DSER102

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR111
DTHR111

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
BLYS116
DLYS116

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR139
DTYR139

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
BLYS22
DLYS22

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon