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3K65

Crystal Structure of Prethombin-2/Fragment-2 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BU1 A 599
ChainResidue
AALA201
AGLY235
AHOH738
AHOH776

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BU1 A 600
ChainResidue
BASN373
ALYS236
AHOH663
AHOH673
AHOH706
BLEU366

Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdgdeegvWC
ChainResidueDetails
APHE218-CYS231

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
BLEU359-CYS364

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsDomain: {"description":"Kringle 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Cleavage; by factor Xa","evidences":[{"source":"PubMed","id":"34265300","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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