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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9KMC

Cryo-EM structure of the heterotrimeric interleukin-2 receptor in complex with interleukin-2 and anti-CD25 Fab S417

Functional Information from GO Data
ChainGOidnamespacecontents
D0002366biological_processleukocyte activation involved in immune response
D0002639biological_processpositive regulation of immunoglobulin production
D0002903biological_processnegative regulation of B cell apoptotic process
D0005125molecular_functioncytokine activity
D0005134molecular_functioninterleukin-2 receptor binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005893cellular_componentinterleukin-2 receptor complex
D0006955biological_processimmune response
D0007155biological_processcell adhesion
D0007186biological_processG protein-coupled receptor signaling pathway
D0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
D0007204biological_processpositive regulation of cytosolic calcium ion concentration
D0007259biological_processcell surface receptor signaling pathway via JAK-STAT
D0007267biological_processcell-cell signaling
D0008083molecular_functiongrowth factor activity
D0008284biological_processpositive regulation of cell population proliferation
D0019209molecular_functionkinase activator activity
D0030101biological_processnatural killer cell activation
D0030217biological_processT cell differentiation
D0030246molecular_functioncarbohydrate binding
D0030307biological_processpositive regulation of cell growth
D0030890biological_processpositive regulation of B cell proliferation
D0031851molecular_functionkappa-type opioid receptor binding
D0032740biological_processpositive regulation of interleukin-17 production
D0034105biological_processpositive regulation of tissue remodeling
D0038110biological_processinterleukin-2-mediated signaling pathway
D0042102biological_processpositive regulation of T cell proliferation
D0042104biological_processpositive regulation of activated T cell proliferation
D0043066biological_processnegative regulation of apoptotic process
D0043208molecular_functionglycosphingolipid binding
D0045471biological_processresponse to ethanol
D0045582biological_processpositive regulation of T cell differentiation
D0045591biological_processpositive regulation of regulatory T cell differentiation
D0045621biological_processpositive regulation of lymphocyte differentiation
D0050729biological_processpositive regulation of inflammatory response
D0060999biological_processpositive regulation of dendritic spine development
D0070665biological_processpositive regulation of leukocyte proliferation
D0097696biological_processcell surface receptor signaling pathway via STAT
D1900100biological_processpositive regulation of plasma cell differentiation
D1901327biological_processresponse to tacrolimus
D1902107biological_processpositive regulation of leukocyte differentiation
D2000320biological_processnegative regulation of T-helper 17 cell differentiation
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
ETYR200-HIS206
FTYR191-HIS197
site_idPS00424
Number of Residues13
DetailsINTERLEUKIN_2 Interleukin-2 signature. TELkhLqCLeeEL
ChainResidueDetails
DTHR71-LEU83
site_idPS01355
Number of Residues32
DetailsHEMATOPO_REC_S_F1 Short hematopoietin receptor family 1 signature. LtpdtqyefqVRvkplqgeftt..........WSpWSqplaF
ChainResidueDetails
BLEU198-PHE229
CVAL213-TRP246
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsDomain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues63
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"3134887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues100
DetailsDomain: {"description":"Fibronectin type-III","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsMotif: {"description":"WSXWS motif"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16477002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16293754","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16477002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","featureId":"CAR_000051","evidences":[{"source":"PubMed","id":"2793860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6333684","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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