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3US3

Recombinant rabbit skeletal calsequestrin-MPD complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005509molecular_functioncalcium ion binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
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
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A 368
ChainResidue
APHE6
APRO7
ATRP242
ATYR298
ATRP299

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MRD A 369
ChainResidue
AHOH493
AGLN63
ALEU294
ALEU295
AHOH462

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 370
ChainResidue
AASN279
AGLU344
AHOH413

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD A 371
ChainResidue
AVAL314
AASN316
AASP321
AVAL346
AGLY349
AGLU350

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 372
ChainResidue
AASN17
AVAL18
ALEU74
AASP80
AHOH490

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 373
ChainResidue
AGLU199
ATHR229
ATHR277
AHOH756

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 374
ChainResidue
AASP210
APRO212
AGLU217
AHOH391

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 375
ChainResidue
ATHR189
AHOH474
AHOH565
AHOH684
AHOH801

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 376
ChainResidue
APRO172
AHOH629
AHOH771

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

226707

PDB entries from 2024-10-30

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