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9GSH

Cryo-EM structure of PMCA-NPTN complex captured in E1-Ca-ATP state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000902biological_processcell morphogenesis
A0005388molecular_functionP-type calcium transporter activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0007423biological_processsensory organ development
A0007595biological_processlactation
A0007605biological_processsensory perception of sound
A0007626biological_processlocomotory behavior
A0008361biological_processregulation of cell size
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0021549biological_processcerebellum development
A0021692biological_processcerebellar Purkinje cell layer morphogenesis
A0021702biological_processcerebellar Purkinje cell differentiation
A0021707biological_processcerebellar granule cell differentiation
A0030165molecular_functionPDZ domain binding
A0030182biological_processneuron differentiation
A0030425cellular_componentdendrite
A0030899molecular_functioncalcium-dependent ATPase activity
A0032591cellular_componentdendritic spine membrane
A0032809cellular_componentneuronal cell body membrane
A0035254molecular_functionglutamate receptor binding
A0040011biological_processlocomotion
A0042428biological_processserotonin metabolic process
A0042472biological_processinner ear morphogenesis
A0042734cellular_componentpresynaptic membrane
A0043025cellular_componentneuronal cell body
A0045202cellular_componentsynapse
A0045211cellular_componentpostsynaptic membrane
A0045299biological_processotolith mineralization
A0046068biological_processcGMP metabolic process
A0046872molecular_functionmetal ion binding
A0048167biological_processregulation of synaptic plasticity
A0048787cellular_componentpresynaptic active zone membrane
A0048839biological_processinner ear development
A0050808biological_processsynapse organization
A0050885biological_processneuromuscular process controlling balance
A0050910biological_processdetection of mechanical stimulus involved in sensory perception of sound
A0051480biological_processregulation of cytosolic calcium ion concentration
A0051928biological_processpositive regulation of calcium ion transport
A0060088biological_processauditory receptor cell stereocilium organization
A0060113biological_processinner ear receptor cell differentiation
A0090102biological_processcochlea development
A0098684cellular_componentphotoreceptor ribbon synapse
A0098688cellular_componentparallel fiber to Purkinje cell synapse
A0098839cellular_componentpostsynaptic density membrane
A0098978cellular_componentglutamatergic synapse
A0098982cellular_componentGABA-ergic synapse
A0099566biological_processregulation of postsynaptic cytosolic calcium ion concentration
A1905059molecular_functionP-type calcium transporter activity involved in regulation of postsynaptic cytosolic calcium ion concentration
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP454-THR460

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues200
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues67
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues450
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"Q9Y639","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues86
DetailsDomain: {"description":"Ig-like 2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues90
DetailsDomain: {"description":"Ig-like 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsRegion: {"description":"Narpin; mediates binding with FGFR1 and has antidepressant-like activity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16944957","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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