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3TLM

Crystal Structure of Endoplasmic Reticulum Ca2+-ATPase (SERCA) From Bovine Muscle

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005388molecular_functionP-type calcium transporter activity
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0016020cellular_componentmembrane
A0016529cellular_componentsarcoplasmic reticulum
A0016887molecular_functionATP hydrolysis activity
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AVAL304
AALA305
AILE307
AGLU309
AASN795
AASP799

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP799
AGLU907
AHOH1028
AASN767
AGLU770
ATHR798

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 1005
ChainResidue
AASP351
ATHR353
AASP702
AACP1001
AHOH1011
AHOH1012

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K A 1006
ChainResidue
ALEU710
ALYS711
AALA713
AGLU731

site_idAC5
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ACP A 1001
ChainResidue
AASP351
ATHR353
AGLU442
APHE487
AARG489
ALYS514
AGLY515
AALA516
AARG559
ALEU561
ATHR624
AGLY625
AASP626
AARG677
ALYS683
AMG1005
AHOH1014

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":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues63
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues31
DetailsRegion: {"description":"Interaction with PLN","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues19
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22387132","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TLM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64578","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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