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4ZLK

Crystal structure of mouse myosin-5a in complex with calcium-bound calmodulin

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
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0008076cellular_componentvoltage-gated potassium channel complex
B0008179molecular_functionadenylate cyclase binding
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030426cellular_componentgrowth cone
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031800molecular_functiontype 3 metabotropic glutamate receptor binding
B0031966cellular_componentmitochondrial membrane
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0044305cellular_componentcalyx of Held
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050998molecular_functionnitric-oxide synthase binding
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
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0097225cellular_componentsperm midpiece
B0098901biological_processregulation of cardiac muscle cell action potential
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B1902494cellular_componentcatalytic complex
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA B 201
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BGLU31

site_idAC2
Number of Residues5
Detailsbinding site for residue CA B 202
ChainResidue
BGLU67
BASP56
BASP58
BASN60
BTHR62

site_idAC3
Number of Residues5
Detailsbinding site for residue CA B 203
ChainResidue
BASP93
BASP95
BASN97
BTYR99
BGLU104

site_idAC4
Number of Residues5
Detailsbinding site for residue CA B 204
ChainResidue
BASP129
BASP131
BASP133
BGLN135
BGLU140

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP20-LEU32
BASP56-PHE68
BASP93-LEU105
BASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0007744|PDB:4HEX, ECO:0007744|PDB:4ZLK
ChainResidueDetails
BASP20
BASP22
BASP24
BTHR26
BGLU31
BASP56
BASP58
BASN60
BTHR62
BGLU67
BASP93
BASP95
BASN97
BTYR99
BGLU104
BASP129
BASP131
BASP133
BGLN135
BGLU140

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.5
ChainResidueDetails
BALA1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:23806337
ChainResidueDetails
BLYS21

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
BTHR44

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BSER81

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BLYS94

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455, ECO:0007744|PubMed:21183079
ChainResidueDetails
BTYR99

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
BSER101

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BTHR110

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BLYS115

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
BTYR138

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
BLYS21

221051

PDB entries from 2024-06-12

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