1YCP
THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16
Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0005509 | molecular_function | calcium ion binding |
H | 0006508 | biological_process | proteolysis |
H | 0007596 | biological_process | blood coagulation |
J | 0004252 | molecular_function | serine-type endopeptidase activity |
J | 0005576 | cellular_component | extracellular region |
J | 0006508 | biological_process | proteolysis |
J | 0007596 | biological_process | blood coagulation |
K | 0004252 | molecular_function | serine-type endopeptidase activity |
K | 0005509 | molecular_function | calcium ion binding |
K | 0006508 | biological_process | proteolysis |
K | 0007596 | biological_process | blood coagulation |
L | 0004252 | molecular_function | serine-type endopeptidase activity |
L | 0005576 | cellular_component | extracellular region |
L | 0006508 | biological_process | proteolysis |
L | 0007596 | biological_process | blood coagulation |
M | 0004252 | molecular_function | serine-type endopeptidase activity |
M | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | BINDING SITE FOR CHAIN F OF FIBRINOPEPTIDE A-ALPHA |
Chain | Residue |
F | HOH450 |
H | GLU97 |
H | LEU99 |
H | ILE174 |
H | ASP189 |
H | ALA190 |
H | CYS191 |
H | GLU192 |
H | GLY193 |
H | SER195 |
H | SER214 |
F | HOH481 |
H | TRP215 |
H | GLY216 |
H | GLY219 |
H | HOH411 |
F | HOH482 |
F | HOH668 |
H | LEU41 |
H | HIS57 |
H | TYR60 |
H | TRP96 |
H | LYS97 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR CHAIN N OF FIBRINOPEPTIDE A-ALPHA |
Chain | Residue |
H | TRP60 |
H | HOH504 |
K | HIS57 |
K | LYS97 |
K | GLU97 |
K | HOH442 |
K | HOH495 |
M | ILE174 |
M | ASP189 |
M | GLU192 |
M | GLY193 |
M | SER195 |
M | SER214 |
M | TRP215 |
M | GLY216 |
M | GLY219 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
Chain | Residue | Details |
K | LEU53-CYS58 | |
H | LEU53-CYS58 |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
Chain | Residue | Details |
M | ASP189-VAL200 | |
H | ASP189-VAL200 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 44 |
Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Active site: {"description":"Charge relay system"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1975","firstPage":"25","lastPage":"46","publisher":"Leiden University Press","address":"Leiden","bookName":"Boerhaave symposium on prothrombin and related coagulation factors","editors":["Hemker H.C.","Veltkamp J.J."],"authors":["Magnusson S.","Sottrup-Jensen L.","Petersen T.E.","Claeys H."]}}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Site: {"description":"Cleavage; by thrombin; to release fibrinopeptide A"} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | ASP102 | |
H | SER195 | |
H | GLY193 | |
H | HIS57 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | ASP102 | |
H | HIS57 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | SER195 | |
H | GLY193 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
M | SER195 | |
M | GLY193 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | SER195 | |
H | GLY196 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
M | SER195 | |
M | GLY196 | |
K | ASP102 | |
K | HIS57 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | ASP102 | |
H | SER195 | |
H | HIS57 |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | ASP102 | |
H | SER195 | |
H | HIS57 | |
H | GLY196 |