1IU4
Crystal Structure Analysis of the Microbial Transglutaminase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
| B | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
| C | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
| D | 0003810 | molecular_function | protein-glutamine gamma-glutamyltransferase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 160 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Active site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 12221081 |
| Chain | Residue | Details |
| A | TRP272 | |
| A | CYS64 | |
| A | CYS64 | |
| A | LYS269 | |
| A | HIS274 | |
| A | ASP255 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 12221081 |
| Chain | Residue | Details |
| B | TRP272 | |
| B | CYS64 | |
| B | CYS64 | |
| B | LYS269 | |
| B | HIS274 | |
| B | ASP255 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 12221081 |
| Chain | Residue | Details |
| C | TRP272 | |
| C | CYS64 | |
| C | CYS64 | |
| C | LYS269 | |
| C | HIS274 | |
| C | ASP255 |
| site_id | CSA4 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 12221081 |
| Chain | Residue | Details |
| D | TRP272 | |
| D | CYS64 | |
| D | CYS64 | |
| D | LYS269 | |
| D | HIS274 | |
| D | ASP255 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| A | CYS64 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ASP255 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | TRP272 | electrostatic stabiliser |
| A | HIS274 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| B | CYS64 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ASP255 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | TRP272 | electrostatic stabiliser |
| B | HIS274 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| C | CYS64 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASP255 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | TRP272 | electrostatic stabiliser |
| C | HIS274 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| D | CYS64 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASP255 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | TRP272 | electrostatic stabiliser |
| D | HIS274 | electrostatic stabiliser, hydrogen bond donor |
