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 | 0005737 | cellular_component | cytoplasm |
| A | 0007596 | biological_process | blood coagulation |
| A | 0018149 | biological_process | peptide cross-linking |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0031093 | cellular_component | platelet alpha granule lumen |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0007596 | biological_process | blood coagulation |
| B | 0018149 | biological_process | peptide cross-linking |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0031093 | cellular_component | platelet alpha granule lumen |
| 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 | 6 |
| Details | binding site for residue CA A 801 |
| Chain | Residue |
| A | ASN436 |
| A | ALA457 |
| A | GLU485 |
| A | GLU490 |
| A | HOH959 |
| A | HOH982 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 802 |
| Chain | Residue |
| A | ASP271 |
| A | HOH943 |
| A | ALA264 |
| A | ASN267 |
| A | LYS269 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 803 |
| Chain | Residue |
| A | ASP343 |
| A | ASP345 |
| A | ASN347 |
| A | GLN349 |
| A | ASP351 |
| A | ASP367 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 804 |
| Chain | Residue |
| A | TYR194 |
| A | LEU195 |
| A | ASP196 |
| A | TRP379 |
| A | PHE559 |
| A | THR561 |
| A | HOH935 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 805 |
| Chain | Residue |
| A | PHE53 |
| A | ASP58 |
| A | THR59 |
| A | TYR83 |
| A | ARG143 |
| A | HOH978 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 806 |
| Chain | Residue |
| A | VAL50 |
| A | SER173 |
| A | ASN175 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 807 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 808 |
| Chain | Residue |
| A | HIS51 |
| A | LEU52 |
| A | PHE53 |
| A | LYS54 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 809 |
| Chain | Residue |
| A | SER250 |
| A | GLY251 |
| A | ASN254 |
| A | LYS257 |
| A | HOH927 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 801 |
| Chain | Residue |
| B | ASP343 |
| B | ASP345 |
| B | ASN347 |
| B | GLN349 |
| B | ASP351 |
| B | ASP367 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 802 |
| Chain | Residue |
| B | ASN436 |
| B | ALA457 |
| B | GLU485 |
| B | GLU490 |
| B | HOH941 |
| B | HOH993 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 803 |
| Chain | Residue |
| B | TYR194 |
| B | ASP196 |
| B | TRP379 |
| B | PHE559 |
| B | THR561 |
| B | HOH956 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 804 |
| Chain | Residue |
| B | PHE53 |
| B | ASP58 |
| B | THR59 |
| B | ARG143 |
| B | HOH952 |
| B | HOH1016 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 805 |
| Chain | Residue |
| B | HIS51 |
| B | LEU52 |
| B | PHE53 |
| B | LYS54 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 806 |
| Chain | Residue |
| B | SER250 |
| B | GLY251 |
| B | ASN254 |
| B | LYS257 |
| B | HOH974 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 807 |
| Chain | Residue |
| B | ALA264 |
| B | ASN267 |
| B | LYS269 |
| B | ASP271 |
| B | HOH991 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for Di-peptide 7NX K 1 and PHE K 2 |
| Chain | Residue |
| A | ASN371 |
| K | ONL3 |
| K | VAL4 |
| site_id | AD9 |
| Number of Residues | 9 |
| Details | binding site for Di-peptide PHE K 2 and ONL K 3 |
| Chain | Residue |
| A | TRP279 |
| A | GLN313 |
| A | CYS314 |
| A | TRP370 |
| A | ASN371 |
| A | TYR372 |
| A | HIS373 |
| K | 7NX1 |
| K | VAL4 |
| site_id | AE1 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide ONL K 3 and VAL K 4 |
| Chain | Residue |
| A | HIS373 |
| K | PHE2 |
| K | LYS5 |
| K | VAL6 |
| A | TRP279 |
| A | GLN313 |
| A | CYS314 |
| A | TRP370 |
| A | ASN371 |
| A | TYR372 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for Di-peptide GLY K 8 and NH2 K 9 |
| Chain | Residue |
| A | THR365 |
| A | ASP367 |
| K | ILE7 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for Di-peptide 7NX O 1 and PHE O 2 |
| Chain | Residue |
| B | TYR214 |
| B | ASN371 |
| O | ONL3 |
| O | VAL4 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide PHE O 2 and ONL O 3 |
| Chain | Residue |
| B | TRP279 |
| B | CYS314 |
| B | TRP370 |
| B | ASN371 |
| B | TYR372 |
| O | 7NX1 |
| O | VAL4 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for Di-peptide ONL O 3 and VAL O 4 |
| Chain | Residue |
| B | TRP279 |
| B | CYS314 |
| B | TRP370 |
| B | ASN371 |
| B | TYR372 |
| O | PHE2 |
| O | LYS5 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for Di-peptide GLY O 8 and NH2 O 9 |
| Chain | Residue |
| B | THR365 |
| B | ASP367 |
| O | LYS5 |
| O | ILE7 |
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 | Site: {"description":"Cleavage; by thrombin; to produce active factor XIII-A"} |
| site_id | SWS_FT_FI4 |
| 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 | 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 |
5MHL
