Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5C73

ATP-driven lipid-linked oligosaccharide flippase PglK in outward-occluded conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0046872molecular_functionmetal ion binding
A0055085biological_processtransmembrane transport
A0140359molecular_functionABC-type transporter activity
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005886cellular_componentplasma membrane
B0006869biological_processlipid transport
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
B0042626molecular_functionATPase-coupled transmembrane transporter activity
B0046872molecular_functionmetal ion binding
B0055085biological_processtransmembrane transport
B0140359molecular_functionABC-type transporter activity
C0000166molecular_functionnucleotide binding
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006869biological_processlipid transport
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
C0042626molecular_functionATPase-coupled transmembrane transporter activity
C0046872molecular_functionmetal ion binding
C0055085biological_processtransmembrane transport
C0140359molecular_functionABC-type transporter activity
F0000166molecular_functionnucleotide binding
F0005524molecular_functionATP binding
F0005886cellular_componentplasma membrane
F0006869biological_processlipid transport
F0016020cellular_componentmembrane
F0016887molecular_functionATP hydrolysis activity
F0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
F0042626molecular_functionATPase-coupled transmembrane transporter activity
F0046872molecular_functionmetal ion binding
F0055085biological_processtransmembrane transport
F0140359molecular_functionABC-type transporter activity
G0000166molecular_functionnucleotide binding
G0005524molecular_functionATP binding
G0005886cellular_componentplasma membrane
G0006869biological_processlipid transport
G0016020cellular_componentmembrane
G0016887molecular_functionATP hydrolysis activity
G0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
G0042626molecular_functionATPase-coupled transmembrane transporter activity
G0046872molecular_functionmetal ion binding
G0055085biological_processtransmembrane transport
G0140359molecular_functionABC-type transporter activity
K0000166molecular_functionnucleotide binding
K0005524molecular_functionATP binding
K0005886cellular_componentplasma membrane
K0006869biological_processlipid transport
K0016020cellular_componentmembrane
K0016887molecular_functionATP hydrolysis activity
K0034040molecular_functionATPase-coupled lipid transmembrane transporter activity
K0042626molecular_functionATPase-coupled transmembrane transporter activity
K0046872molecular_functionmetal ion binding
K0055085biological_processtransmembrane transport
K0140359molecular_functionABC-type transporter activity
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL
ChainResidueDetails
CLEU485-LEU499

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues768
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26266984","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1290
DetailsDomain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2214
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"26266984","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues324
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"26266984","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1812
DetailsDomain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues126
DetailsRegion: {"description":"Important for stimulation of ATPase activity by lipid-linked oligosaccharides and subsequent translocation of lipid-linked oligosaccharides","evidences":[{"source":"PubMed","id":"26266984","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon