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 | 0007599 | biological_process | hemostasis |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0018149 | biological_process | peptide cross-linking |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0072378 | biological_process | blood coagulation, fibrin clot formation |
| A | 0072562 | cellular_component | blood microparticle |
| 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 | 0007599 | biological_process | hemostasis |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0018149 | biological_process | peptide cross-linking |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0031093 | cellular_component | platelet alpha granule lumen |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0072378 | biological_process | blood coagulation, fibrin clot formation |
| B | 0072562 | cellular_component | blood microparticle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE YB A 732 |
| Chain | Residue |
| A | ASN436 |
| A | GLU485 |
| A | GLU490 |
| A | HOH3006 |
| A | HOH5034 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE YB B 732 |
| Chain | Residue |
| B | ASN436 |
| B | GLU485 |
| B | GLU490 |
| B | YB744 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE YB A 733 |
| Chain | Residue |
| A | ASP270 |
| A | ASP271 |
| A | YB740 |
| A | YB741 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE YB A 740 |
| Chain | Residue |
| A | ASP271 |
| A | YB733 |
| B | YB742 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE YB A 741 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE YB B 742 |
| Chain | Residue |
| A | YB740 |
| B | ASP270 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE YB B 744 |
| Chain | Residue |
| B | ASN436 |
| B | ASP438 |
| B | ALA457 |
| B | GLU485 |
| B | YB732 |
| site_id | CAT |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD IN CHAIN A |
| Chain | Residue |
| A | CYS314 |
| A | HIS373 |
| A | ASP396 |
| site_id | CBT |
| Number of Residues | 3 |
| Details | CATALYTIC TRIAD IN CHAIN B |
| Chain | Residue |
| B | CYS314 |
| B | HIS373 |
| B | ASP396 |
| site_id | INA |
| Number of Residues | 4 |
| Details | ION BINDING SITE A YTTERBIUM LIGANDS |
| Chain | Residue |
| A | GLU490 |
| A | ALA457 |
| A | ASN436 |
| A | GLU485 |
| site_id | INB |
| Number of Residues | 4 |
| Details | ION BINDING SITE B YTTERBIUM LIGANDS |
| Chain | Residue |
| B | ALA457 |
| B | ASN436 |
| B | GLU485 |
| B | GLU490 |
| site_id | YB4 |
| Number of Residues | 4 |
| Details | MINOR YTTERBIUM BINDING SITE ON DIMER 2-FOLD AXIS |
| Chain | Residue |
| A | ASP270 |
| A | GLU272 |
| B | ASP270 |
| B | GLU272 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"7913750","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9988734","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
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 | 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 |
