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 |