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6LCR

Cryo-EM structure of Dnf1 from Chaetomium thermophilum in the E1-ATP state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0010008cellular_componentendosome membrane
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0090554molecular_functionphosphatidylcholine floppase activity
A0090555molecular_functionphosphatidylethanolamine flippase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP606-THR612

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues73
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BMET1-LYS48
BPHE381-SER407
ASER559-MET1123
AASP1168-TYR1200
ATYR1259-ASP1262
ALYS1324-MET1555

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BLEU49-THR69
ALEU1303-VAL1323
BILE360-PHE380
AVAL492-ILE512
APHE538-ILE558
AILE1124-PHE1144
ATHR1147-LEU1167
AMET1201-LEU1221
ALEU1238-THR1258
ATRP1263-TYR1283

site_idSWS_FT_FI3
Number of Residues289
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BTYR70-GLY359
AALA513-GLY537
AGLU1145-TYR1146
ATHR1222-ARG1237
ATHR1284-GLU1302

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
BASN131
BASN189
BASN219
BASN232
BASN241
BASN314

site_idSWS_FT_FI5
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9Y2Q0
ChainResidueDetails
AASP606
ATHR608
APHE781
AASP1057
AASN1060

site_idSWS_FT_FI6
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P32660
ChainResidueDetails
ALYS607
AGLU740
ASER783
AARG839
ATHR840
ATHR919
AARG1031
ALYS1037

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P39524
ChainResidueDetails
ALYS786

site_idSWS_FT_FI8
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04191
ChainResidueDetails
ALYS804
AGLY920
AASP921

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8NB49
ChainResidueDetails
AASP1061

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:32303992, ECO:0007744|PDB:6LCP
ChainResidueDetails
AARG1320

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Involved in the release of the transported lipid into the cytosolic leaflet => ECO:0000250|UniProtKB:C7EXK4
ChainResidueDetails
AILE554

225946

PDB entries from 2024-10-09

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