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3V1W

Molecular Basis for Multiple Ligand Binding of Calsequestrin and Potential Inhibition by Caffeine and Gallocatecin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005509molecular_functioncalcium ion binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005783cellular_componentendoplasmic reticulum
A0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0016020cellular_componentmembrane
A0016529cellular_componentsarcoplasmic reticulum
A0030018cellular_componentZ disc
A0030955molecular_functionpotassium ion binding
A0033017cellular_componentsarcoplasmic reticulum membrane
A0033018cellular_componentsarcoplasmic reticulum lumen
A0042803molecular_functionprotein homodimerization activity
A0045214biological_processsarcomere organization
A0046872molecular_functionmetal ion binding
A0051258biological_processprotein polymerization
A0051279biological_processregulation of release of sequestered calcium ion into cytosol
A0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
A1901341biological_processpositive regulation of store-operated calcium channel activity
A2001256biological_processregulation of store-operated calcium entry
Functional Information from PROSITE/UniProt
site_idPS00863
Number of Residues15
DetailsCALSEQUESTRIN_1 Calsequestrin signature 1. EEGLDFPeYDGvDRV
ChainResidueDetails
AGLU1-VAL15

site_idPS00864
Number of Residues20
DetailsCALSEQUESTRIN_2 Calsequestrin signature 2. ELEDWLEDVLeGeINTEDDD
ChainResidueDetails
AGLU338-ASP357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P19633
ChainResidueDetails
ATYR9

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P19633
ChainResidueDetails
ASER47
ASER182

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P19633
ChainResidueDetails
ATHR90

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22170046
ChainResidueDetails
AASN316

237735

PDB entries from 2025-06-18

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