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1IMV

2.85 A crystal structure of PEDF

Functional Information from GO Data
ChainGOidnamespacecontents
A0001822biological_processkidney development
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0007614biological_processshort-term memory
A0010447biological_processresponse to acidic pH
A0010596biological_processnegative regulation of endothelial cell migration
A0010629biological_processnegative regulation of gene expression
A0010976biological_processpositive regulation of neuron projection development
A0014070biological_processresponse to organic cyclic compound
A0016525biological_processnegative regulation of angiogenesis
A0030424cellular_componentaxon
A0042470cellular_componentmelanosome
A0042698biological_processovulation cycle
A0043025cellular_componentneuronal cell body
A0043203cellular_componentaxon hillock
A0046685biological_processresponse to arsenic-containing substance
A0048471cellular_componentperinuclear region of cytoplasm
A0050769biological_processpositive regulation of neurogenesis
A0060041biological_processretina development in camera-type eye
A0060767biological_processepithelial cell proliferation involved in prostate gland development
A0060770biological_processnegative regulation of epithelial cell proliferation involved in prostate gland development
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0071279biological_processcellular response to cobalt ion
A0071300biological_processcellular response to retinoic acid
A0071333biological_processcellular response to glucose stimulus
A0071549biological_processcellular response to dexamethasone stimulus
A1901652biological_processresponse to peptide
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. YHLNQPFIFvL
ChainResidueDetails
ATYR368-LEU378

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:15374885
ChainResidueDetails
ASER4
ASER94

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:15374885
ChainResidueDetails
ASER207

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:11562499, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN265

218500

PDB entries from 2024-04-17

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