1L9M
Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions change structure for activation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005198 | molecular_function | structural molecule activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0018149 | biological_process | peptide cross-linking |
| A | 0030216 | biological_process | keratinocyte differentiation |
| A | 0031069 | biological_process | hair follicle morphogenesis |
| A | 0031234 | cellular_component | extrinsic component of cytoplasmic side of plasma membrane |
| A | 0031424 | biological_process | keratinization |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0036211 | biological_process | protein modification process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005198 | molecular_function | structural molecule activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016746 | molecular_function | acyltransferase activity |
| B | 0018149 | biological_process | peptide cross-linking |
| B | 0030216 | biological_process | keratinocyte differentiation |
| B | 0031069 | biological_process | hair follicle morphogenesis |
| B | 0031234 | cellular_component | extrinsic component of cytoplasmic side of plasma membrane |
| B | 0031424 | biological_process | keratinization |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0036211 | biological_process | protein modification process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BR A 700 |
| Chain | Residue |
| A | ARG169 |
| A | ARG587 |
| A | ILE589 |
| A | ILE590 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 701 |
| Chain | Residue |
| A | ASP183 |
| A | SER186 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 702 |
| Chain | Residue |
| A | ASN229 |
| A | HOH977 |
| A | ALA221 |
| A | ASN224 |
| A | ASN226 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BR B 703 |
| Chain | Residue |
| B | ARG169 |
| B | ARG587 |
| B | ILE589 |
| B | ILE590 |
| B | HOH1093 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 704 |
| Chain | Residue |
| B | ASP183 |
| B | SER186 |
| B | HOH773 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 705 |
| Chain | Residue |
| B | ALA221 |
| B | ASN224 |
| B | SER225 |
| B | ASN226 |
| B | ASN229 |
| B | HOH1001 |
Functional Information from PROSITE/UniProt
| site_id | PS00547 |
| Number of Residues | 18 |
| Details | TRANSGLUTAMINASES Transglutaminases active site. GQCWVfAGTlnTaLRSLG |
| Chain | Residue | Details |
| A | GLY270-GLY287 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10024 |
| Chain | Residue | Details |
| A | CYS272 | |
| A | HIS330 | |
| A | ASP353 | |
| B | CYS272 | |
| B | HIS330 | |
| B | ASP353 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11980702, ECO:0000269|PubMed:12679341 |
| Chain | Residue | Details |
| A | ALA221 | |
| A | ASP324 | |
| A | ASN393 | |
| A | SER415 | |
| A | GLU443 | |
| A | GLU448 | |
| B | ALA221 | |
| B | ASN224 | |
| B | ASN226 | |
| B | ASP227 | |
| B | ASN229 | |
| A | ASN224 | |
| B | ASP301 | |
| B | ASP303 | |
| B | ASN305 | |
| B | SER307 | |
| B | ASP324 | |
| B | ASN393 | |
| B | SER415 | |
| B | GLU443 | |
| B | GLU448 | |
| A | ASN226 | |
| A | ASP227 | |
| A | ASN229 | |
| A | ASP301 | |
| A | ASP303 | |
| A | ASN305 | |
| A | SER307 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by CTSL |
| Chain | Residue | Details |
| A | ALA466 | |
| B | ALA466 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.7 |
| Chain | Residue | Details |
| A | ALA1 | |
| B | ALA1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | TYR110 | |
| B | TYR110 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
| Chain | Residue | Details |
| A | THR111 | |
| B | THR111 |
