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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 Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
BHIS363
BASP419
BALA525

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
ChainResidueDetails
BARG320

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
BASN373

227344

PDB entries from 2024-11-13

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