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1LKJ

NMR Structure of Apo Calmodulin from Yeast Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000131cellular_componentincipient cellular bud site
A0000742biological_processkaryogamy involved in conjugation with cellular fusion
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005816cellular_componentspindle pole body
A0005823cellular_componentcentral plaque of spindle pole body
A0005856cellular_componentcytoskeleton
A0005933cellular_componentcellular bud
A0005934cellular_componentcellular bud tip
A0005935cellular_componentcellular bud neck
A0006606biological_processprotein import into nucleus
A0006661biological_processphosphatidylinositol biosynthetic process
A0006897biological_processendocytosis
A0006898biological_processreceptor-mediated endocytosis
A0007010biological_processcytoskeleton organization
A0007114biological_processcell budding
A0010968biological_processregulation of microtubule nucleation
A0016237biological_processmicroautophagy
A0016460cellular_componentmyosin II complex
A0030050biological_processvesicle transport along actin filament
A0030234molecular_functionenzyme regulator activity
A0030479cellular_componentactin cortical patch
A0031475cellular_componentmyosin V complex
A0042144biological_processvacuole fusion, non-autophagic
A0043332cellular_componentmating projection tip
A0045160cellular_componentmyosin I complex
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0051019molecular_functionmitogen-activated protein kinase binding
A0051300biological_processspindle pole body organization
A1903525biological_processregulation of membrane tubulation
A2000601biological_processpositive regulation of Arp2/3 complex-mediated actin nucleation
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDNNGSISssEL
ChainResidueDetails
AASP20-LEU32
AASP56-PHE68
AASP93-LEU105

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP20
AGLU67
AASP93
AASN95
AASP97
AGLU104
AASP22
AASN24
ASER26
AGLU31
AASP56
AASP58
AASN60
AGLN62

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER81

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER101

218853

PDB entries from 2024-04-24

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