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 | 0005515 | molecular_function | protein 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 | 0005515 | molecular_function | protein 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 | Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10024","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11980702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12679341","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1g0d |
| Chain | Residue | Details |
| A | ASP353 | |
| A | CYS272 | |
| A | TYR525 | |
| A | HIS330 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1g0d |
| Chain | Residue | Details |
| B | ASP353 | |
| B | CYS272 | |
| B | TYR525 | |
| B | HIS330 |
