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3O3U

Crystal Structure of Human Receptor for Advanced Glycation Endproducts (RAGE)

Functional Information from GO Data
ChainGOidnamespacecontents
N0005515molecular_functionprotein binding
N0006974biological_processDNA damage response
N0008643biological_processcarbohydrate transport
N0015144molecular_functioncarbohydrate transmembrane transporter activity
N0015768biological_processmaltose transport
N0016020cellular_componentmembrane
N0030288cellular_componentouter membrane-bounded periplasmic space
N0034219biological_processcarbohydrate transmembrane transport
N0034289biological_processdetection of maltose stimulus
N0042597cellular_componentperiplasmic space
N0042956biological_processmaltodextrin transmembrane transport
N0043190cellular_componentATP-binding cassette (ABC) transporter complex
N0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
N0055085biological_processtransmembrane transport
N0060326biological_processcell chemotaxis
N1901982molecular_functionmaltose binding
N1990060cellular_componentmaltose transport complex
Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
NPRO107-ASN124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
NASN1025
NASN1081

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PDB entries from 2025-06-11

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