Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0005737 | cellular_component | cytoplasm |
A | 0007596 | biological_process | blood coagulation |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0018149 | biological_process | peptide cross-linking |
A | 0031093 | cellular_component | platelet alpha granule lumen |
A | 0046872 | molecular_function | metal ion binding |
A | 0062023 | cellular_component | collagen-containing extracellular matrix |
A | 0072378 | biological_process | blood coagulation, fibrin clot formation |
A | 0072562 | cellular_component | blood microparticle |
A | 1990234 | cellular_component | transferase complex |
B | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0007596 | biological_process | blood coagulation |
B | 0016746 | molecular_function | acyltransferase activity |
B | 0018149 | biological_process | peptide cross-linking |
B | 0031093 | cellular_component | platelet alpha granule lumen |
B | 0046872 | molecular_function | metal ion binding |
B | 0062023 | cellular_component | collagen-containing extracellular matrix |
B | 0072378 | biological_process | blood coagulation, fibrin clot formation |
B | 0072562 | cellular_component | blood microparticle |
B | 1990234 | cellular_component | transferase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | binding site for residue CA A 801 |
Chain | Residue |
A | ALA264 |
A | ASN267 |
A | LYS269 |
A | ASP271 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 802 |
Chain | Residue |
A | ASP367 |
A | ASP343 |
A | ASP345 |
A | ASN347 |
A | GLN349 |
A | ASP351 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CA A 803 |
Chain | Residue |
A | ASN436 |
A | ASP438 |
A | ALA457 |
A | GLU485 |
A | GLU490 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 804 |
Chain | Residue |
A | HIS51 |
A | LEU52 |
A | PHE53 |
A | LYS54 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue CA B 801 |
Chain | Residue |
B | ALA264 |
B | ASN267 |
B | LYS269 |
B | ASP271 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA B 802 |
Chain | Residue |
B | ASP343 |
B | ASP345 |
B | ASN347 |
B | GLN349 |
B | ASP351 |
B | ASP367 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue CA B 803 |
Chain | Residue |
B | ASN436 |
B | ALA457 |
B | GLU485 |
B | GLU490 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 804 |
Chain | Residue |
B | HIS51 |
B | LEU52 |
B | PHE53 |
B | LYS54 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 805 |
Chain | Residue |
B | LYS269 |
B | ASP270 |
B | ARG681 |
site_id | AD1 |
Number of Residues | 10 |
Details | binding site for residues TRM G 1 and 1TX G 2 |
Chain | Residue |
A | TYR214 |
A | ARG223 |
A | TRP279 |
A | CYS314 |
A | TRP370 |
A | ASN371 |
A | TYR372 |
A | HIS373 |
A | GLN400 |
G | LEU3 |
site_id | AD2 |
Number of Residues | 10 |
Details | binding site for Di-peptide 1TX G 2 and LEU G 3 |
Chain | Residue |
A | TRP279 |
A | CYS314 |
A | TRP370 |
A | ASN371 |
A | TYR372 |
A | HIS373 |
A | GLN400 |
G | TRM1 |
G | ILE4 |
G | LEU5 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residues TRM H 1 and 1TX H 2 |
Chain | Residue |
B | ARG223 |
B | TRP279 |
B | CYS314 |
B | TRP315 |
B | TRP370 |
B | ASN371 |
B | TYR372 |
B | HIS373 |
B | GLN400 |
H | LEU3 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for Di-peptide 1TX H 2 and LEU H 3 |
Chain | Residue |
B | TRP279 |
B | CYS314 |
B | TRP370 |
B | ASN371 |
B | TYR372 |
B | HIS373 |
B | GLN400 |
H | TRM1 |
H | ILE4 |
H | LEU5 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for Di-peptide PRO H 8 and NH2 H 9 |
Chain | Residue |
B | TYR441 |
H | PRO6 |
H | TRP7 |
Functional Information from PROSITE/UniProt
site_id | PS00547 |
Number of Residues | 18 |
Details | TRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGVfnTfLRCLG |
Chain | Residue | Details |
A | GLY312-GLY329 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | CYS314 | |
A | HIS373 | |
A | ASP396 | |
B | CYS314 | |
B | HIS373 | |
B | ASP396 | |
Chain | Residue | Details |
A | ASN436 | |
A | ASP438 | |
A | GLU485 | |
A | GLU490 | |
B | ASN436 | |
B | ASP438 | |
B | GLU485 | |
B | GLU490 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by thrombin; to produce active factor XIII-A |
Chain | Residue | Details |
A | ARG37 | |
B | ARG37 | |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
Chain | Residue | Details |
A | ASN613 | |
B | ASN613 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 149 |
Chain | Residue | Details |
A | TRP279 | electrostatic stabiliser, hydrogen bond donor |
A | CYS314 | electrostatic stabiliser |
A | HIS373 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASP396 | electrostatic stabiliser, hydrogen bond acceptor |
A | TYR560 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 149 |
Chain | Residue | Details |
B | TRP279 | electrostatic stabiliser, hydrogen bond donor |
B | CYS314 | electrostatic stabiliser |
B | HIS373 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ASP396 | electrostatic stabiliser, hydrogen bond acceptor |
B | TYR560 | electrostatic stabiliser, hydrogen bond donor |