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7YAJ

CryoEM structure of SPCA1a in E1-Mn-AMPPCP state subclass 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005388molecular_functionP-type calcium transporter activity
A0005524molecular_functionATP binding
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006816biological_processcalcium ion transport
A0006828biological_processmanganese ion transport
A0006874biological_processintracellular calcium ion homeostasis
A0008544biological_processepidermis development
A0016020cellular_componentmembrane
A0016339biological_processcalcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules
A0016887molecular_functionATP hydrolysis activity
A0030036biological_processactin cytoskeleton organization
A0032468biological_processGolgi calcium ion homeostasis
A0032472biological_processGolgi calcium ion transport
A0032580cellular_componentGolgi cisterna membrane
A0033106cellular_componentcis-Golgi network membrane
A0042998biological_processpositive regulation of Golgi to plasma membrane protein transport
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0046872molecular_functionmetal ion binding
A0070588biological_processcalcium ion transmembrane transport
A0071421biological_processmanganese ion transmembrane transport
A0098629biological_processtrans-Golgi network membrane organization
A0140613molecular_functionP-type manganese transporter activity
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP350-THR356

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues646
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250
ChainResidueDetails
AMET1-PRO70
ASER124-MET262
AVAL313-ILE699
AVAL751-ILE770
AGLN829-ASN841
ALYS897-VAL919

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250
ChainResidueDetails
ALEU71-ALA91

site_idSWS_FT_FI3
Number of Residues60
DetailsTOPO_DOM: Lumenal => ECO:0000250
ChainResidueDetails
AVAL92-VAL104
AVAL283-MET294
AALA720-LEU729
APHE794-THR808
APHE861-ILE875

site_idSWS_FT_FI4
Number of Residues18
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250
ChainResidueDetails
ASER105-ARG123

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250
ChainResidueDetails
AASP263-LEU282

site_idSWS_FT_FI6
Number of Residues17
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250
ChainResidueDetails
APHE295-ILE312

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250
ChainResidueDetails
ALYS700-LEU719

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250
ChainResidueDetails
AASN730-GLY750

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250
ChainResidueDetails
ALEU771-VAL793

site_idSWS_FT_FI10
Number of Residues19
DetailsTRANSMEM: Helical; Name=8 => ECO:0000250
ChainResidueDetails
ATHR809-SER828

site_idSWS_FT_FI11
Number of Residues18
DetailsTRANSMEM: Helical; Name=9 => ECO:0000250
ChainResidueDetails
AARG842-TYR860

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=10 => ECO:0000250
ChainResidueDetails
ALEU876-LYS896

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250
ChainResidueDetails
AASP350

site_idSWS_FT_FI14
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AVAL303
AALA304
AILE306
AGLU308
AASP644
AASP648
AASN738
AASP742

220113

PDB entries from 2024-05-22

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