Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6XMT

Structure of P5A-ATPase Spf1, BeF3-bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005801cellular_componentcis-Golgi network
A0006874biological_processintracellular calcium ion homeostasis
A0015031biological_processprotein transport
A0015662molecular_functionP-type ion transporter activity
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
A0030026biological_processintracellular manganese ion homeostasis
A0034214biological_processprotein hexamerization
A0043335biological_processprotein unfolding
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0055092biological_processsterol homeostasis
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0098655biological_processmonoatomic cation transmembrane transport
A0140358molecular_functionP-type transmembrane transporter activity
A0140567molecular_functionmembrane protein dislocase activity
A0140569biological_processextraction of mislocalized protein from ER membrane
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue BEF A 1301
ChainResidue
AGLY309
AASP487
ATHR489
ATHR697
ALYS797
AASN819
AMG1302

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 1302
ChainResidue
AASP816
AGLY817
ABEF1301
AASP487
ATHR489

Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP487-THR493

site_idPS01229
Number of Residues23
DetailsCOF_2 Hypothetical cof family signature 2. CGDGtNDvgaLkqAhvGiaLlnG
ChainResidueDetails
ACYS814-GLY836

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues838
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:32973005
ChainResidueDetails
AMET1-PRO27
ATRP77-THR188
AARG247-ASP395
APHE465-VAL971
ASER1036-ASN1055
AGLN1122-ASN1133
AMET1198-LYS1215

site_idSWS_FT_FI2
Number of Residues15
DetailsTRANSMEM: Helical; Name=TMa => ECO:0000305|PubMed:32973005
ChainResidueDetails
ATYR28-TYR43

site_idSWS_FT_FI3
Number of Residues49
DetailsTOPO_DOM: Lumenal => ECO:0000305|PubMed:32973005
ChainResidueDetails
APHE44-TRP56
APHE217
AARG426-ILE427
AALA1012-GLY1017
APRO1085-SER1099
ATHR1152-THR1168

site_idSWS_FT_FI4
Number of Residues19
DetailsTRANSMEM: Helical; Name=TMb => ECO:0000305|PubMed:32973005
ChainResidueDetails
ATHR57-ALA76

site_idSWS_FT_FI5
Number of Residues27
DetailsTRANSMEM: Helical; Name=TM1 => ECO:0000305|PubMed:32973005
ChainResidueDetails
APHE189-GLU216

site_idSWS_FT_FI6
Number of Residues28
DetailsTRANSMEM: Helical; Name=TM2 => ECO:0000305|PubMed:32973005
ChainResidueDetails
ATRP218-PHE246

site_idSWS_FT_FI7
Number of Residues29
DetailsTRANSMEM: Helical; Name=TM3 => ECO:0000305|PubMed:32973005
ChainResidueDetails
AASN396-GLY425

site_idSWS_FT_FI8
Number of Residues14
DetailsTRANSMEM: Helical; Name=TM4a => ECO:0000305|PubMed:32973005
ChainResidueDetails
AGLN428-VAL442

site_idSWS_FT_FI9
Number of Residues18
DetailsTRANSMEM: Helical; Name=TM4b => ECO:0000305|PubMed:32973005
ChainResidueDetails
AGLU446-LYS464

site_idSWS_FT_FI10
Number of Residues39
DetailsTRANSMEM: Helical; Name=TM5 => ECO:0000305|PubMed:32973005
ChainResidueDetails
ASER972-MET1011

site_idSWS_FT_FI11
Number of Residues17
DetailsTRANSMEM: Helical; Name=TM6 => ECO:0000305|PubMed:32973005
ChainResidueDetails
AASP1018-ILE1035

site_idSWS_FT_FI12
Number of Residues28
DetailsTRANSMEM: Helical; Name=TM7 => ECO:0000305|PubMed:32973005
ChainResidueDetails
AVAL1056-GLU1084

site_idSWS_FT_FI13
Number of Residues21
DetailsTRANSMEM: Helical; Name=TM8 => ECO:0000305|PubMed:32973005
ChainResidueDetails
ALEU1100-TYR1121

site_idSWS_FT_FI14
Number of Residues17
DetailsTRANSMEM: Helical; Name=TM9 => ECO:0000305|PubMed:32973005
ChainResidueDetails
ALYS1134-ALA1151

site_idSWS_FT_FI15
Number of Residues28
DetailsTRANSMEM: Helical; Name=TM10 => ECO:0000305|PubMed:32973005
ChainResidueDetails
AASP1169-PHE1197

site_idSWS_FT_FI16
Number of Residues1
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000305|PubMed:22745129, ECO:0000305|PubMed:24392018, ECO:0000305|PubMed:30785834, ECO:0000305|PubMed:32353073
ChainResidueDetails
AASP487

site_idSWS_FT_FI17
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:32973005
ChainResidueDetails
AASP487
ATHR489
AARG634
AASP699
AASP816

site_idSWS_FT_FI18
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y2Q0
ChainResidueDetails
APHE582

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER324
ASER936

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon