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5MPM

SERCA2a from pig heart

Functional Information from GO Data
ChainGOidnamespacecontents
A0000045biological_processautophagosome assembly
A0000166molecular_functionnucleotide binding
A0003012biological_processmuscle system process
A0005215molecular_functiontransporter activity
A0005246molecular_functioncalcium channel regulator activity
A0005388molecular_functionP-type calcium transporter activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0006937biological_processregulation of muscle contraction
A0008016biological_processregulation of heart contraction
A0010882biological_processregulation of cardiac muscle contraction by calcium ion signaling
A0016020cellular_componentmembrane
A0016240biological_processautophagosome membrane docking
A0016529cellular_componentsarcoplasmic reticulum
A0016887molecular_functionATP hydrolysis activity
A0019899molecular_functionenzyme binding
A0032469biological_processendoplasmic reticulum calcium ion homeostasis
A0032470biological_processpositive regulation of endoplasmic reticulum calcium ion concentration
A0033017cellular_componentsarcoplasmic reticulum membrane
A0044325molecular_functiontransmembrane transporter binding
A0044548molecular_functionS100 protein binding
A0046872molecular_functionmetal ion binding
A0070588biological_processcalcium ion transmembrane transport
A0086036biological_processregulation of cardiac muscle cell membrane potential
A0086039molecular_functionP-type calcium transporter activity involved in regulation of cardiac muscle cell membrane potential
A0097470cellular_componentribbon synapse
A0106222molecular_functionlncRNA binding
A0140056biological_processorganelle localization by membrane tethering
A1903515biological_processcalcium ion transport from cytosol to endoplasmic reticulum
A1990036biological_processcalcium ion import into sarcoplasmic reticulum
A1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue MGF A 1001
ChainResidue
AGLY182
AHOH1101
AHOH1104
AASP351
ALYS352
ATHR353
ATHR624
AGLY625
ALYS683
AASN705
AMG1004

site_idAC2
Number of Residues15
Detailsbinding site for residue CZA A 1002
ChainResidue
AGLN56
APHE57
AASP59
ALEU61
AVAL62
ALEU65
ALEU98
AASN101
AALA102
ALEU253
AILE307
APRO308
AMG1003
AHOH1102
AHOH1103

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 1003
ChainResidue
AGLN56
ACZA1002
AHOH1102
AHOH1103

site_idAC4
Number of Residues7
Detailsbinding site for residue MG A 1004
ChainResidue
AGLY182
AASP351
ATHR353
AASP702
AMGF1001
AHOH1104
AHOH1105

site_idAC5
Number of Residues4
Detailsbinding site for residue K A 1005
ChainResidue
ALEU710
ALYS711
ASER713
AGLU731

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 Residues662
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues108
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues19
DetailsRegion: {"description":"Interaction with HAX1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues31
DetailsRegion: {"description":"Interaction with PLN","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30777856","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6HXB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30777856","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MPM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O55143","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P16615","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P16615","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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