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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1320 |
| Chain | Residue |
| A | ASN436 |
| A | ASP438 |
| A | ALA457 |
| A | HOH1518 |
| A | HOH1646 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 1321 |
| Chain | Residue |
| B | HOH1417 |
| B | HOH1536 |
| B | HOH1692 |
| B | ASN436 |
| B | SER437 |
| B | ASP438 |
| B | ALA457 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1330 |
| Chain | Residue |
| A | ASP456 |
| A | THR458 |
| A | HIS459 |
| A | LYS462 |
| A | LYS621 |
| A | HOH1473 |
| A | HOH1550 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1331 |
| Chain | Residue |
| B | ASP456 |
| B | THR458 |
| B | HIS459 |
| B | LYS462 |
| B | LYS621 |
| B | HOH1372 |
| B | HOH1595 |
| B | HOH1664 |
| B | HOH1867 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1332 |
| Chain | Residue |
| B | ASN517 |
| B | SER543 |
| B | HIS544 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGO A 1340 |
| Chain | Residue |
| A | ARG260 |
| A | ASP404 |
| A | TYR407 |
| A | ARG408 |
| A | HOH1376 |
| A | HOH1386 |
| B | ASP404 |
| B | ARG408 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGO A 1341 |
| Chain | Residue |
| A | GLN85 |
| A | MET136 |
| A | GLU138 |
| A | SER141 |
| A | VAL142 |
| A | ARG143 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PGO A 1342 |
| Chain | Residue |
| A | TYR500 |
| B | PHE424 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGO B 1343 |
| Chain | Residue |
| B | GLU525 |
| B | LYS534 |
| B | HOH1760 |
| B | HOH1964 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGO B 1344 |
| Chain | Residue |
| B | LYS565 |
| B | GLY596 |
| B | GLN597 |
| B | HOH2068 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGO B 1345 |
| Chain | Residue |
| B | GLU571 |
| B | GLU585 |
| B | ALA586 |
| B | VAL587 |
| B | HOH1438 |
| B | HOH1732 |
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 | TRP315 | |
| A | CYS374 | |
| A | SER397 | |
| B | TRP315 | |
| B | CYS374 | |
| B | SER397 | |
| Chain | Residue | Details |
| A | SER437 | |
| A | LEU439 | |
| A | GLY486 | |
| A | ARG491 | |
| B | SER437 | |
| B | LEU439 | |
| B | GLY486 | |
| B | ARG491 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by thrombin; to produce active factor XIII-A |
| Chain | Residue | Details |
| A | GLY38 | |
| B | GLY38 | |
| Chain | Residue | Details |
| A | GLU2 | |
| B | GLU2 | |
| Chain | Residue | Details |
| A | GLU614 | |
| B | GLU614 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1g0d |
| Chain | Residue | Details |
| A | CYS314 | |
| A | ASP396 | |
| A | HIS373 | |
| A | TYR560 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1g0d |
| Chain | Residue | Details |
| B | CYS314 | |
| B | ASP396 | |
| B | HIS373 | |
| B | TYR560 | |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 149 |
| Chain | Residue | Details |
| A | ASP280 | electrostatic stabiliser, hydrogen bond donor |
| A | TRP315 | electrostatic stabiliser |
| A | CYS374 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER397 | electrostatic stabiliser, hydrogen bond acceptor |
| A | THR561 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 149 |
| Chain | Residue | Details |
| B | ASP280 | electrostatic stabiliser, hydrogen bond donor |
| B | TRP315 | electrostatic stabiliser |
| B | CYS374 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER397 | electrostatic stabiliser, hydrogen bond acceptor |
| B | THR561 | electrostatic stabiliser, hydrogen bond donor |
