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1E9J

SOLUTION STRUCTURE OF THE A-SUBUNIT OF HUMAN CHORIONIC GONADOTROPIN [INCLUDING A SINGLE GLCNAC RESIDUE AT ASN52 AND ASN78]

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005796cellular_componentGolgi lumen
A0006590biological_processthyroid hormone generation
A0007186biological_processG protein-coupled receptor signaling pathway
A0008284biological_processpositive regulation of cell population proliferation
A0008406biological_processgonad development
A0009755biological_processhormone-mediated signaling pathway
A0010469biological_processregulation of signaling receptor activity
A0010893biological_processpositive regulation of steroid biosynthetic process
A0016913molecular_functionfollicle-stimulating hormone activity
A0016914cellular_componentfollicle-stimulating hormone complex
A0030335biological_processpositive regulation of cell migration
A0030878biological_processthyroid gland development
A0032275biological_processluteinizing hormone secretion
A0032870biological_processcellular response to hormone stimulus
A0035265biological_processorgan growth
A0042699biological_processfollicle-stimulating hormone signaling pathway
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046621biological_processnegative regulation of organ growth
A0046884biological_processfollicle-stimulating hormone secretion
A0048589biological_processdevelopmental growth
A0061696cellular_componentpituitary gonadotropin complex
Functional Information from PROSITE/UniProt
site_idPS00779
Number of Residues13
DetailsGLYCO_HORMONE_ALPHA_1 Glycoprotein hormones alpha chain signature 1. CmGCCFSRAYPTP
ChainResidueDetails
ACYS28-PRO40

site_idPS00780
Number of Residues14
DetailsGLYCO_HORMONE_ALPHA_2 Glycoprotein hormones alpha chain signature 2. NHTaChCsTCyyHK
ChainResidueDetails
AASN78-LYS91

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15662415, ECO:0000269|PubMed:24692546, ECO:0007744|PDB:4MQW
ChainResidueDetails
AASN52
AASN78

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PDB entries from 2024-11-06

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