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4KYT

The structure of superinhibitory phospholamban bound to the calcium pump SERCA1a

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005388molecular_functionP-type calcium transporter activity
A0005509molecular_functioncalcium ion binding
A0005524molecular_functionATP binding
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0016020cellular_componentmembrane
A0016529cellular_componentsarcoplasmic reticulum
A0016887molecular_functionATP hydrolysis activity
A0031448biological_processpositive regulation of fast-twitch skeletal muscle fiber contraction
A0033017cellular_componentsarcoplasmic reticulum membrane
A0046872molecular_functionmetal ion binding
A0070588biological_processcalcium ion transmembrane transport
A0106134biological_processpositive regulation of cardiac muscle cell contraction
A1901896biological_processpositive regulation of ATPase-coupled calcium transmembrane transporter activity
A1902082biological_processpositive regulation of calcium ion import into sarcoplasmic reticulum
A1990036biological_processcalcium ion import into sarcoplasmic reticulum
B0001675biological_processacrosome assembly
B0002026biological_processregulation of the force of heart contraction
B0005739cellular_componentmitochondrion
B0005789cellular_componentendoplasmic reticulum membrane
B0006874biological_processintracellular calcium ion homeostasis
B0007219biological_processNotch signaling pathway
B0007283biological_processspermatogenesis
B0008016biological_processregulation of heart contraction
B0008542biological_processvisual learning
B0010459biological_processnegative regulation of heart rate
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016529cellular_componentsarcoplasmic reticulum
B0031966cellular_componentmitochondrial membrane
B0032780biological_processnegative regulation of ATP-dependent activity
B0033017cellular_componentsarcoplasmic reticulum membrane
B0042030molecular_functionATPase inhibitor activity
B0042803molecular_functionprotein homodimerization activity
B0045475biological_processlocomotor rhythm
B0045822biological_processnegative regulation of heart contraction
B0046716biological_processmuscle cell cellular homeostasis
B0048738biological_processcardiac muscle tissue development
B0050802biological_processcircadian sleep/wake cycle, sleep
B0051924biological_processregulation of calcium ion transport
B0051926biological_processnegative regulation of calcium ion transport
B0086004biological_processregulation of cardiac muscle cell contraction
B0086023biological_processadenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process
B0086092biological_processregulation of the force of heart contraction by cardiac conduction
B0090279biological_processregulation of calcium ion import
B0090534cellular_componentcalcium ion-transporting ATPase complex
B1901020biological_processnegative regulation of calcium ion transmembrane transporter activity
B1901077biological_processregulation of relaxation of muscle
B1901894biological_processregulation of ATPase-coupled calcium transmembrane transporter activity
B1901895biological_processnegative regulation of ATPase-coupled calcium transmembrane transporter activity
B1902081biological_processnegative regulation of calcium ion import into sarcoplasmic reticulum
C0001675biological_processacrosome assembly
C0002026biological_processregulation of the force of heart contraction
C0005739cellular_componentmitochondrion
C0005789cellular_componentendoplasmic reticulum membrane
C0006874biological_processintracellular calcium ion homeostasis
C0007219biological_processNotch signaling pathway
C0007283biological_processspermatogenesis
C0008016biological_processregulation of heart contraction
C0008542biological_processvisual learning
C0010459biological_processnegative regulation of heart rate
C0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0016020cellular_componentmembrane
C0016529cellular_componentsarcoplasmic reticulum
C0031966cellular_componentmitochondrial membrane
C0032780biological_processnegative regulation of ATP-dependent activity
C0033017cellular_componentsarcoplasmic reticulum membrane
C0042030molecular_functionATPase inhibitor activity
C0042803molecular_functionprotein homodimerization activity
C0045475biological_processlocomotor rhythm
C0045822biological_processnegative regulation of heart contraction
C0046716biological_processmuscle cell cellular homeostasis
C0048738biological_processcardiac muscle tissue development
C0050802biological_processcircadian sleep/wake cycle, sleep
C0051924biological_processregulation of calcium ion transport
C0051926biological_processnegative regulation of calcium ion transport
C0086004biological_processregulation of cardiac muscle cell contraction
C0086023biological_processadenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process
C0086092biological_processregulation of the force of heart contraction by cardiac conduction
C0090279biological_processregulation of calcium ion import
C0090534cellular_componentcalcium ion-transporting ATPase complex
C1901020biological_processnegative regulation of calcium ion transmembrane transporter activity
C1901077biological_processregulation of relaxation of muscle
C1901894biological_processregulation of ATPase-coupled calcium transmembrane transporter activity
C1901895biological_processnegative regulation of ATPase-coupled calcium transmembrane transporter activity
C1902081biological_processnegative regulation of calcium ion import into sarcoplasmic reticulum
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP351-THR357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues663
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:10864315
ChainResidueDetails
AMET1-SER48
AASN111-LEU253
AVAL314-MET757
APHE809-LEU828
AGLU918-ASN930

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:10864315
ChainResidueDetails
ALEU49-ALA69
CPHE32-LEU52

site_idSWS_FT_FI3
Number of Residues108
DetailsTOPO_DOM: Lumenal => ECO:0000269|PubMed:10864315
ChainResidueDetails
ACYS70-VAL89
AILE274-TYR295
ATHR778-LEU787
AALA852-MET897
AVAL950-LEU964

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:10864315
ChainResidueDetails
AGLU90-ARG110
CSER16

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:10864315
ChainResidueDetails
AASP254-LEU273
CTHR17

site_idSWS_FT_FI6
Number of Residues17
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:10864315
ChainResidueDetails
APHE296-ALA313
CCYS36

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:10864315
ChainResidueDetails
ALYS758-LEU777

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:10864315
ChainResidueDetails
AILE788-GLY808

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:10864315
ChainResidueDetails
AILE829-ALA851

site_idSWS_FT_FI10
Number of Residues19
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:10864315
ChainResidueDetails
ATHR898-SER917

site_idSWS_FT_FI11
Number of Residues18
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:10864315
ChainResidueDetails
AILE931-TYR949

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:10864315
ChainResidueDetails
ATHR965-LYS985

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:18075584
ChainResidueDetails
AASP351

site_idSWS_FT_FI14
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AVAL304

site_idSWS_FT_FI15
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AALA305

site_idSWS_FT_FI16
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU
ChainResidueDetails
AILE307

site_idSWS_FT_FI17
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AGLU309

site_idSWS_FT_FI18
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:1WPG, ECO:0007744|PDB:1XP5, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:2ZBE, ECO:0007744|PDB:2ZBF, ECO:0007744|PDB:2ZBG, ECO:0007744|PDB:3AR8, ECO:0007744|PDB:3AR9, ECO:0007744|PDB:3B9B, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N5K, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:5A3Q, ECO:0007744|PDB:5A3S
ChainResidueDetails
AASP351
ATHR353
AASP703

site_idSWS_FT_FI19
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3AR3, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8
ChainResidueDetails
AGLU442

site_idSWS_FT_FI20
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:1WPG, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8
ChainResidueDetails
AARG489

site_idSWS_FT_FI21
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C8K, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU
ChainResidueDetails
ALYS515

site_idSWS_FT_FI22
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2BY4, ECO:0007744|PDB:2C88, ECO:0007744|PDB:2C8K, ECO:0007744|PDB:2DQS, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3B9R, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4H1W, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU
ChainResidueDetails
AARG560

site_idSWS_FT_FI23
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8
ChainResidueDetails
ATHR625

site_idSWS_FT_FI24
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4UU1, ECO:0007744|PDB:4XOU
ChainResidueDetails
AGLY626

site_idSWS_FT_FI25
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0007744|PDB:1T5T
ChainResidueDetails
AASP627

site_idSWS_FT_FI26
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3FGO, ECO:0007744|PDB:3FPB, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4BEW, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA8
ChainResidueDetails
AARG678

site_idSWS_FT_FI27
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU
ChainResidueDetails
ALYS684

site_idSWS_FT_FI28
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU
ChainResidueDetails
AASN706

site_idSWS_FT_FI29
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AASN768
ATHR799

site_idSWS_FT_FI30
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AGLU771

site_idSWS_FT_FI31
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AASN796

site_idSWS_FT_FI32
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5T, ECO:0007744|PDB:1VFP, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:2ZBD, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:3N8G, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU, ECO:0007744|PDB:5XA7, ECO:0007744|PDB:5XA8
ChainResidueDetails
AASP800

site_idSWS_FT_FI33
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:26175901, ECO:0007744|PDB:1SU4, ECO:0007744|PDB:1T5S, ECO:0007744|PDB:2C9M, ECO:0007744|PDB:3AR2, ECO:0007744|PDB:3BA6, ECO:0007744|PDB:4NAB, ECO:0007744|PDB:4XOU
ChainResidueDetails
AGLU908

site_idSWS_FT_FI34
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q64578
ChainResidueDetails
ATHR441
ATHR569

site_idSWS_FT_FI35
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64578
ChainResidueDetails
ASER581

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 849
ChainResidueDetails
AASP351covalent catalysis
AASP703metal ligand
AASP707metal ligand

226707

PDB entries from 2024-10-30

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