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2R9Y

Structure of antiplasmin

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0002034biological_processmaintenance of blood vessel diameter homeostasis by renin-angiotensin
A0004866molecular_functionendopeptidase inhibitor activity
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005576cellular_componentextracellular region
A0005577cellular_componentfibrinogen complex
A0005615cellular_componentextracellular space
A0006953biological_processacute-phase response
A0009986cellular_componentcell surface
A0010757biological_processnegative regulation of plasminogen activation
A0030199biological_processcollagen fibril organization
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0032967biological_processpositive regulation of collagen biosynthetic process
A0042803molecular_functionprotein homodimerization activity
A0045597biological_processpositive regulation of cell differentiation
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046330biological_processpositive regulation of JNK cascade
A0048514biological_processblood vessel morphogenesis
A0048661biological_processpositive regulation of smooth muscle cell proliferation
A0050820biological_processpositive regulation of coagulation
A0051496biological_processpositive regulation of stress fiber assembly
A0051918biological_processnegative regulation of fibrinolysis
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071636biological_processpositive regulation of transforming growth factor beta production
Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FTVNRPFLFfI
ChainResidueDetails
APHE382-ILE392

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSite: {"description":"Reactive bond for chymotrypsin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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