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1PVH

Crystal structure of leukemia inhibitory factor in complex with gp130

Functional Information from GO Data
ChainGOidnamespacecontents
B0005102molecular_functionsignaling receptor binding
B0005125molecular_functioncytokine activity
B0005146molecular_functionleukemia inhibitory factor receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005829cellular_componentcytosol
B0006955biological_processimmune response
B0008083molecular_functiongrowth factor activity
B0008284biological_processpositive regulation of cell population proliferation
B0010646biological_processregulation of cell communication
B0023051biological_processregulation of signaling
B0030154biological_processcell differentiation
B0030225biological_processmacrophage differentiation
B0033138biological_processpositive regulation of peptidyl-serine phosphorylation
B0033630biological_processpositive regulation of cell adhesion mediated by integrin
B0043410biological_processpositive regulation of MAPK cascade
B0045595biological_processregulation of cell differentiation
B0045651biological_processpositive regulation of macrophage differentiation
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046888biological_processnegative regulation of hormone secretion
B0048861biological_processleukemia inhibitory factor signaling pathway
B0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
B0051240biological_processpositive regulation of multicellular organismal process
B0072108biological_processpositive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis
B0072307biological_processregulation of metanephric nephron tubule epithelial cell differentiation
B0097696biological_processcell surface receptor signaling pathway via STAT
B1904894biological_processpositive regulation of receptor signaling pathway via STAT
B2000026biological_processregulation of multicellular organismal development
D0005102molecular_functionsignaling receptor binding
D0005125molecular_functioncytokine activity
D0005146molecular_functionleukemia inhibitory factor receptor binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005829cellular_componentcytosol
D0006955biological_processimmune response
D0008083molecular_functiongrowth factor activity
D0008284biological_processpositive regulation of cell population proliferation
D0010646biological_processregulation of cell communication
D0023051biological_processregulation of signaling
D0030154biological_processcell differentiation
D0030225biological_processmacrophage differentiation
D0033138biological_processpositive regulation of peptidyl-serine phosphorylation
D0033630biological_processpositive regulation of cell adhesion mediated by integrin
D0043410biological_processpositive regulation of MAPK cascade
D0045595biological_processregulation of cell differentiation
D0045651biological_processpositive regulation of macrophage differentiation
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0046888biological_processnegative regulation of hormone secretion
D0048861biological_processleukemia inhibitory factor signaling pathway
D0050731biological_processpositive regulation of peptidyl-tyrosine phosphorylation
D0051240biological_processpositive regulation of multicellular organismal process
D0072108biological_processpositive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis
D0072307biological_processregulation of metanephric nephron tubule epithelial cell differentiation
D0097696biological_processcell surface receptor signaling pathway via STAT
D1904894biological_processpositive regulation of receptor signaling pathway via STAT
D2000026biological_processregulation of multicellular organismal development
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE IOD A 302
ChainResidue
ATRP288

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IOD D 202
ChainResidue
CTRP288
DGLY140

Functional Information from PROSITE/UniProt
site_idPS00590
Number of Residues20
DetailsLIF_OSM LIF / OSM family signature. SgkdvFQkKklgCqLLgkYK
ChainResidueDetails
BSER151-LYS170

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues182
DetailsDomain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"WSXWS motif"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11098061","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11098061","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20489211","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8489250","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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