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5CRG

Human skeletal calsequestrin, D210G mutant high-calcium complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005783cellular_componentendoplasmic reticulum
A0005790cellular_componentsmooth endoplasmic reticulum
A0007519biological_processskeletal muscle tissue development
A0014701cellular_componentjunctional sarcoplasmic reticulum membrane
A0014802cellular_componentterminal cisterna
A0014804cellular_componentterminal cisterna lumen
A0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A0014870biological_processresponse to muscle inactivity
A0014894biological_processresponse to denervation involved in regulation of muscle adaptation
A0016529cellular_componentsarcoplasmic reticulum
A0030016cellular_componentmyofibril
A0030018cellular_componentZ disc
A0030315cellular_componentT-tubule
A0031674cellular_componentI band
A0033017cellular_componentsarcoplasmic reticulum membrane
A0033018cellular_componentsarcoplasmic reticulum lumen
A0042383cellular_componentsarcolemma
A0042802molecular_functionidentical protein binding
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
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005783cellular_componentendoplasmic reticulum
B0005790cellular_componentsmooth endoplasmic reticulum
B0007519biological_processskeletal muscle tissue development
B0014701cellular_componentjunctional sarcoplasmic reticulum membrane
B0014802cellular_componentterminal cisterna
B0014804cellular_componentterminal cisterna lumen
B0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
B0014870biological_processresponse to muscle inactivity
B0014894biological_processresponse to denervation involved in regulation of muscle adaptation
B0016529cellular_componentsarcoplasmic reticulum
B0030016cellular_componentmyofibril
B0030018cellular_componentZ disc
B0030315cellular_componentT-tubule
B0031674cellular_componentI band
B0033017cellular_componentsarcoplasmic reticulum membrane
B0033018cellular_componentsarcoplasmic reticulum lumen
B0042383cellular_componentsarcolemma
B0042802molecular_functionidentical protein binding
B0045214biological_processsarcomere organization
B0046872molecular_functionmetal ion binding
B0051258biological_processprotein polymerization
B0051279biological_processregulation of release of sequestered calcium ion into cytosol
B0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
B1901341biological_processpositive regulation of store-operated calcium channel activity
B2001256biological_processregulation of store-operated calcium entry
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0005783cellular_componentendoplasmic reticulum
C0005790cellular_componentsmooth endoplasmic reticulum
C0007519biological_processskeletal muscle tissue development
C0014701cellular_componentjunctional sarcoplasmic reticulum membrane
C0014802cellular_componentterminal cisterna
C0014804cellular_componentterminal cisterna lumen
C0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
C0014870biological_processresponse to muscle inactivity
C0014894biological_processresponse to denervation involved in regulation of muscle adaptation
C0016529cellular_componentsarcoplasmic reticulum
C0030016cellular_componentmyofibril
C0030018cellular_componentZ disc
C0030315cellular_componentT-tubule
C0031674cellular_componentI band
C0033017cellular_componentsarcoplasmic reticulum membrane
C0033018cellular_componentsarcoplasmic reticulum lumen
C0042383cellular_componentsarcolemma
C0042802molecular_functionidentical protein binding
C0045214biological_processsarcomere organization
C0046872molecular_functionmetal ion binding
C0051258biological_processprotein polymerization
C0051279biological_processregulation of release of sequestered calcium ion into cytosol
C0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
C1901341biological_processpositive regulation of store-operated calcium channel activity
C2001256biological_processregulation of store-operated calcium entry
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005739cellular_componentmitochondrion
D0005759cellular_componentmitochondrial matrix
D0005783cellular_componentendoplasmic reticulum
D0005790cellular_componentsmooth endoplasmic reticulum
D0007519biological_processskeletal muscle tissue development
D0014701cellular_componentjunctional sarcoplasmic reticulum membrane
D0014802cellular_componentterminal cisterna
D0014804cellular_componentterminal cisterna lumen
D0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
D0014870biological_processresponse to muscle inactivity
D0014894biological_processresponse to denervation involved in regulation of muscle adaptation
D0016529cellular_componentsarcoplasmic reticulum
D0030016cellular_componentmyofibril
D0030018cellular_componentZ disc
D0030315cellular_componentT-tubule
D0031674cellular_componentI band
D0033017cellular_componentsarcoplasmic reticulum membrane
D0033018cellular_componentsarcoplasmic reticulum lumen
D0042383cellular_componentsarcolemma
D0042802molecular_functionidentical protein binding
D0045214biological_processsarcomere organization
D0046872molecular_functionmetal ion binding
D0051258biological_processprotein polymerization
D0051279biological_processregulation of release of sequestered calcium ion into cytosol
D0051281biological_processpositive regulation of release of sequestered calcium ion into cytosol
D1901341biological_processpositive regulation of store-operated calcium channel activity
D2001256biological_processregulation of store-operated calcium entry
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
AASP13
AVAL15
AGLU55
AGLU59
AHOH796
AHOH932

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AHOH769
AHOH846
AHOH893
AGLU199
ATHR229
ATHR277

site_idAC3
Number of Residues7
Detailsbinding site for residue CA A 403
ChainResidue
AGLY210
APRO212
AGLU217
AHOH652
AHOH716
AHOH957
AHOH970

site_idAC4
Number of Residues7
Detailsbinding site for residue CA A 404
ChainResidue
ATHR189
AHOH554
AHOH694
AHOH706
AHOH717
AHOH1008
AHOH1015

site_idAC5
Number of Residues4
Detailsbinding site for residue CA A 405
ChainResidue
AASP5
APHE6
AGLU8
AHOH570

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 406
ChainResidue
AGLU91
AGLU105
AASP107
AGLU240
AHOH531
AHOH711

site_idAC7
Number of Residues6
Detailsbinding site for residue CA A 407
ChainResidue
AGLU91
AASP107
AGLU243
AHOH669
AHOH912
AHOH947

site_idAC8
Number of Residues5
Detailsbinding site for residue CA A 408
ChainResidue
AASP93
AASP107
AHOH719
AHOH912
AHOH1143

site_idAC9
Number of Residues7
Detailsbinding site for residue CA A 409
ChainResidue
AASP113
AHOH646
AHOH822
AHOH1054
BASP113
BHOH503
BHOH557

site_idAD1
Number of Residues6
Detailsbinding site for residue CA A 410
ChainResidue
AGLU117
AHOH894
AHOH920
AHOH946
BASP290
BHOH628

site_idAD2
Number of Residues6
Detailsbinding site for residue CA A 411
ChainResidue
AASP165
AHOH582
AHOH591
AHOH679
AHOH776
AHOH1094

site_idAD3
Number of Residues7
Detailsbinding site for residue CA A 412
ChainResidue
AGLU169
AGLU215
AHOH663
AHOH673
AHOH731
AHOH937
AHOH1029

site_idAD4
Number of Residues7
Detailsbinding site for residue CA A 413
ChainResidue
APRO172
AHOH597
AHOH748
AHOH824
AHOH936
AHOH1011
AHOH1066

site_idAD5
Number of Residues5
Detailsbinding site for residue CA A 414
ChainResidue
ALYS301
AASP304
AHOH787
AHOH896
AHOH975

site_idAD6
Number of Residues4
Detailsbinding site for residue CA A 415
ChainResidue
AASP321
ATHR353
AHOH778
AHOH997

site_idAD7
Number of Residues7
Detailsbinding site for residue CA A 416
ChainResidue
AASP332
AHOH850
AHOH917
AHOH919
AHOH923
AHOH1002
AHOH1131

site_idAD8
Number of Residues4
Detailsbinding site for residue CA A 417
ChainResidue
AHOH873
AGLU344
AHOH701
AHOH851

site_idAD9
Number of Residues7
Detailsbinding site for residue CA A 418
ChainResidue
AASP290
BASP121
BHOH548
BHOH553
BHOH654
BHOH722
BHOH926

site_idAE1
Number of Residues5
Detailsbinding site for residue CA A 419
ChainResidue
AASP259
AASP261
AGLU330
BGLU128
BHOH882

site_idAE2
Number of Residues6
Detailsbinding site for residue CA A 420
ChainResidue
AASP261
AGLU331
AHOH553
BGLU135
BHOH567
BHOH758

site_idAE3
Number of Residues8
Detailsbinding site for residue CA A 421
ChainResidue
AASP261
AGLU264
AGLU331
AHOH566
AHOH583
AHOH618
BGLU135
BHOH636

site_idAE4
Number of Residues7
Detailsbinding site for residue CA A 422
ChainResidue
AASP121
AHOH561
AHOH627
AHOH683
AHOH741
BASP290
BHOH917

site_idAE5
Number of Residues7
Detailsbinding site for residue CA A 423
ChainResidue
AGLU128
AHOH592
BASP259
BASP261
BGLU330
BHOH501
BHOH546

site_idAE6
Number of Residues6
Detailsbinding site for residue CA A 424
ChainResidue
AGLU135
AHOH593
AHOH695
BASP261
BGLU331
BHOH520

site_idAE7
Number of Residues7
Detailsbinding site for residue CA A 425
ChainResidue
AGLU135
AHOH547
BASP261
BGLU264
BGLU331
BHOH529
BHOH789

site_idAE8
Number of Residues6
Detailsbinding site for residue CA A 426
ChainResidue
AASP290
AHOH705
BGLU117
BHOH695
BHOH791
BHOH896

site_idAE9
Number of Residues6
Detailsbinding site for residue CA B 401
ChainResidue
BASP13
BVAL15
BGLU55
BGLU59
BHOH735
BHOH902

site_idAF1
Number of Residues6
Detailsbinding site for residue CA B 402
ChainResidue
BGLU199
BTHR229
BTHR277
BHOH658
BHOH674
BHOH881

site_idAF2
Number of Residues5
Detailsbinding site for residue CA B 403
ChainResidue
BGLY210
BPRO212
BGLU217
BHOH825
BHOH853

site_idAF3
Number of Residues6
Detailsbinding site for residue CA B 404
ChainResidue
BTHR189
BHOH566
BHOH635
BHOH671
BHOH721
BHOH909

site_idAF4
Number of Residues5
Detailsbinding site for residue CA B 405
ChainResidue
AHOH1076
BASP332
BHOH753
BHOH786
BHOH805

site_idAF5
Number of Residues6
Detailsbinding site for residue CA B 406
ChainResidue
BASP5
BPHE6
BGLU8
BHOH571
BHOH841
BHOH907

site_idAF6
Number of Residues6
Detailsbinding site for residue CA B 407
ChainResidue
BGLU91
BGLU105
BASP107
BGLU240
BHOH625
BHOH645

site_idAF7
Number of Residues6
Detailsbinding site for residue CA B 408
ChainResidue
BGLU91
BASP107
BGLU243
BHOH556
BHOH751
BHOH880

site_idAF8
Number of Residues5
Detailsbinding site for residue CA B 409
ChainResidue
BASP93
BASP107
BHOH556
BHOH751
BHOH756

site_idAF9
Number of Residues4
Detailsbinding site for residue CA B 410
ChainResidue
BGLU102
BGLU169
BHOH580
BHOH906

site_idAG1
Number of Residues6
Detailsbinding site for residue CA B 411
ChainResidue
BGLU169
BGLU215
BHOH779
BHOH783
BHOH897
BHOH906

site_idAG2
Number of Residues7
Detailsbinding site for residue CA B 412
ChainResidue
BASP165
BHOH539
BHOH744
BHOH769
BHOH905
BHOH1043
BHOH1071

site_idAG3
Number of Residues7
Detailsbinding site for residue CA B 413
ChainResidue
BPRO172
BHOH647
BHOH661
BHOH668
BHOH839
BHOH956
BHOH992

site_idAG4
Number of Residues6
Detailsbinding site for residue CA B 414
ChainResidue
BASP245
BASP247
BILE249
BHOH697
BHOH921
BHOH952

site_idAG5
Number of Residues6
Detailsbinding site for residue CA B 415
ChainResidue
BASP321
BTHR353
BHOH846
BHOH862
BHOH901
BHOH976

site_idAG6
Number of Residues6
Detailsbinding site for residue CA C 401
ChainResidue
CASP13
CVAL15
CGLU55
CGLU59
CHOH905
CHOH989

site_idAG7
Number of Residues6
Detailsbinding site for residue CA C 402
ChainResidue
CGLU199
CTHR229
CTHR277
CHOH677
CHOH736
CHOH896

site_idAG8
Number of Residues7
Detailsbinding site for residue CA C 403
ChainResidue
CGLY210
CPRO212
CGLU217
CHOH773
CHOH888
CHOH921
CHOH972

site_idAG9
Number of Residues7
Detailsbinding site for residue CA C 404
ChainResidue
CTHR189
CHOH599
CHOH618
CHOH623
CHOH793
CHOH1001
CHOH1017

site_idAH1
Number of Residues4
Detailsbinding site for residue CA C 405
ChainResidue
CASP5
CPHE6
CGLU8
CHOH524

site_idAH2
Number of Residues6
Detailsbinding site for residue CA C 406
ChainResidue
CGLU91
CGLU105
CASP107
CGLU240
CHOH513
CHOH730

site_idAH3
Number of Residues6
Detailsbinding site for residue CA C 407
ChainResidue
CGLU91
CASP107
CGLU243
CHOH662
CHOH899
CHOH940

site_idAH4
Number of Residues4
Detailsbinding site for residue CA C 408
ChainResidue
CASP93
CASP107
CHOH658
CHOH899

site_idAH5
Number of Residues6
Detailsbinding site for residue CA C 409
ChainResidue
CASP113
CHOH723
CHOH890
CHOH985
DASP113
DHOH784

site_idAH6
Number of Residues6
Detailsbinding site for residue CA C 410
ChainResidue
CGLU117
CHOH822
CHOH882
CHOH973
DASP290
DHOH648

site_idAH7
Number of Residues7
Detailsbinding site for residue CA C 411
ChainResidue
CASP121
CHOH518
CHOH597
CHOH656
CHOH960
DASP290
DHOH544

site_idAH8
Number of Residues5
Detailsbinding site for residue CA C 412
ChainResidue
CASP165
CHOH541
CHOH733
CHOH759
CHOH1148

site_idAH9
Number of Residues7
Detailsbinding site for residue CA C 413
ChainResidue
CGLU169
CGLU215
CHOH504
CHOH588
CHOH802
CHOH977
CHOH995

site_idAI1
Number of Residues7
Detailsbinding site for residue CA C 414
ChainResidue
CPRO172
CHOH671
CHOH705
CHOH829
CHOH833
CHOH1043
CHOH1060

site_idAI2
Number of Residues5
Detailsbinding site for residue CA C 415
ChainResidue
CLYS301
CASP304
CHOH783
CHOH804
CHOH943

site_idAI3
Number of Residues7
Detailsbinding site for residue CA C 416
ChainResidue
CASP321
CTHR353
CHOH894
CHOH917
CHOH942
CHOH1020
CHOH1027

site_idAI4
Number of Residues4
Detailsbinding site for residue CA C 417
ChainResidue
CASP332
CHOH808
CHOH820
CHOH933

site_idAI5
Number of Residues6
Detailsbinding site for residue CA C 418
ChainResidue
CGLU344
CHOH582
CHOH694
CHOH763
CHOH912
CHOH1076

site_idAI6
Number of Residues7
Detailsbinding site for residue CA C 419
ChainResidue
CASP290
DASP121
DHOH625
DHOH630
DHOH709
DHOH824
DHOH889

site_idAI7
Number of Residues6
Detailsbinding site for residue CA C 420
ChainResidue
CASP259
CASP261
CGLU330
CHOH572
DGLU128
DHOH696

site_idAI8
Number of Residues6
Detailsbinding site for residue CA C 421
ChainResidue
CASP261
CGLU331
CHOH572
DGLU135
DHOH570
DHOH657

site_idAI9
Number of Residues8
Detailsbinding site for residue CA C 422
ChainResidue
CASP261
CGLU264
CGLU331
CHOH626
CHOH637
CHOH776
DGLU135
DHOH677

site_idAJ1
Number of Residues6
Detailsbinding site for residue CA C 423
ChainResidue
CGLU128
CHOH717
DASP259
DASP261
DGLU330
DHOH529

site_idAJ2
Number of Residues7
Detailsbinding site for residue CA C 424
ChainResidue
CGLU135
CCA425
CHOH551
CHOH743
DASP261
DGLU331
DHOH634

site_idAJ3
Number of Residues7
Detailsbinding site for residue CA C 425
ChainResidue
CGLU135
CCA424
CHOH615
DASP261
DGLU264
DGLU331
DHOH524

site_idAJ4
Number of Residues6
Detailsbinding site for residue CA C 426
ChainResidue
CASP290
CHOH655
CHOH974
DGLU117
DHOH895
DHOH902

site_idAJ5
Number of Residues6
Detailsbinding site for residue CA D 401
ChainResidue
DASP13
DVAL15
DGLU55
DGLU59
DHOH637
DHOH913

site_idAJ6
Number of Residues6
Detailsbinding site for residue CA D 402
ChainResidue
DGLU199
DTHR229
DTHR277
DHOH622
DHOH838
DHOH877

site_idAJ7
Number of Residues5
Detailsbinding site for residue CA D 403
ChainResidue
DGLY210
DPRO212
DGLU217
DHOH772
DHOH875

site_idAJ8
Number of Residues6
Detailsbinding site for residue CA D 404
ChainResidue
DTHR189
DHOH569
DHOH646
DHOH664
DHOH722
DHOH932

site_idAJ9
Number of Residues5
Detailsbinding site for residue CA D 405
ChainResidue
DASP5
DPHE6
DGLU8
DHOH542
DHOH893

site_idAK1
Number of Residues6
Detailsbinding site for residue CA D 406
ChainResidue
DGLU91
DGLU105
DASP107
DGLU240
DHOH531
DHOH655

site_idAK2
Number of Residues6
Detailsbinding site for residue CA D 407
ChainResidue
DGLU91
DASP107
DGLU243
DHOH584
DHOH833
DHOH878

site_idAK3
Number of Residues4
Detailsbinding site for residue CA D 408
ChainResidue
DASP93
DASP107
DHOH615
DHOH833

site_idAK4
Number of Residues5
Detailsbinding site for residue CA D 409
ChainResidue
DASP165
DHOH718
DHOH795
DHOH841
DHOH1084

site_idAK5
Number of Residues6
Detailsbinding site for residue CA D 410
ChainResidue
DGLU102
DGLU169
DCA411
DHOH853
DHOH896
DHOH959

site_idAK6
Number of Residues7
Detailsbinding site for residue CA D 411
ChainResidue
DGLU169
DGLU215
DCA410
DHOH826
DHOH850
DHOH896
DHOH959

site_idAK7
Number of Residues7
Detailsbinding site for residue CA D 412
ChainResidue
DPRO172
DHOH581
DHOH582
DHOH681
DHOH756
DHOH948
DHOH983

site_idAK8
Number of Residues6
Detailsbinding site for residue CA D 413
ChainResidue
DASP321
DTHR353
DHOH629
DHOH740
DHOH891
DHOH1006

site_idAK9
Number of Residues6
Detailsbinding site for residue CA D 414
ChainResidue
CHOH868
CHOH1000
DASP332
DHOH822
DHOH857
DHOH886

site_idAL1
Number of Residues8
Detailsbinding site for residue CA D 415
ChainResidue
DGLU337
DGLU340
DHOH506
DHOH643
DHOH759
DHOH922
DHOH935
DHOH1005

Functional Information from PROSITE/UniProt
site_idPS00863
Number of Residues15
DetailsCALSEQUESTRIN_1 Calsequestrin signature 1. QEGLDFPeYDGvDRV
ChainResidueDetails
AGLN1-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 Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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