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 | 12 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | LYS95 | |
| D | LYS95 | |
| D | GLY286 | |
| D | PHE305 | |
| A | GLY286 | |
| A | PHE305 | |
| B | LYS95 | |
| B | GLY286 | |
| B | PHE305 | |
| C | LYS95 | |
| C | GLY286 | |
| C | PHE305 |
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 | LYS95 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY286 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | SER303 | electrostatic stabiliser |
| A | PHE305 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| B | LYS95 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY286 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| B | SER303 | electrostatic stabiliser |
| B | PHE305 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| C | LYS95 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | GLY286 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| C | SER303 | electrostatic stabiliser |
| C | PHE305 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 761 |
| Chain | Residue | Details |
| D | LYS95 | covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | GLY286 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| D | SER303 | electrostatic stabiliser |
| D | PHE305 | electrostatic stabiliser, hydrogen bond donor |
