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4HZH

Structure of recombinant Gla-domainless prothrombin mutant S525A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0007596biological_processblood coagulation
B0004252molecular_functionserine-type endopeptidase activity
B0005509molecular_functioncalcium ion binding
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00021
Number of Residues14
DetailsKRINGLE_1 Kringle domain signature. FCRNpdssttgpWC
ChainResidueDetails
APHE113-CYS126
APHE218-CYS231

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU359-CYS364

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS363
AASP419
AALA525
BHIS363
BASP419
BALA525

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by thrombin
ChainResidueDetails
AARG155
BARG155

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Cleavage; by factor Xa => ECO:0000269|PubMed:34265300
ChainResidueDetails
AARG271
AARG320
BARG271
BARG320

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22171320
ChainResidueDetails
AASN78
AASN100
BASN78
BASN100

site_idSWS_FT_FI5
Number of Residues2
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
AASN373
BASN373

219869

PDB entries from 2024-05-15

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