Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3TRP

Crystal structure of recombinant rabbit skeletal calsequestrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005509molecular_functioncalcium ion binding
A0005759cellular_componentmitochondrial matrix
A0005783cellular_componentendoplasmic reticulum
A0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
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 PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MRD A 354
ChainResidue
AASN276
AGLU340
AGLU344
AHOH404
AHOH427

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MRD A 355
ChainResidue
APHE6
ATRP242
ATYR298
ATRP299

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MRD A 356
ChainResidue
ATYR9
AGLN63
ALEU294
ALEU295
AHOH455
AHOH511

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MPD A 357
ChainResidue
AVAL314
AASP321
AGLY349

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 358
ChainResidue
AASP210
APRO212
AGLU217
AHOH435
AHOH436
AHOH440

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 359
ChainResidue
AASN17
AVAL18
ALEU74
ALYS79
AASP80
AHOH367

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 360
ChainResidue
AGLU199
ATHR229
ATHR277
AHOH605
AHOH732

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 361
ChainResidue
ATHR189
AHOH472
AHOH499
AHOH593
AHOH792

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 362
ChainResidue
AGLU109
AASP291
AHOH368

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 363
ChainResidue
APHE118
AASP121
AGLU236
AHOH742

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 364
ChainResidue
AGLU256
AGLU257
AALA258
AASP288
AHOH754
AHOH768

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 365
ChainResidue
APRO172
AHOH418
AHOH437
AHOH438
AHOH439
AHOH441

Functional Information from PROSITE/UniProt
site_idPS00863
Number of Residues15
DetailsCALSEQUESTRIN_1 Calsequestrin signature 1. EEGLDFPeYDGvDRV
ChainResidueDetails
AGLU1-VAL15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22170046","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon