1A79
CRYSTAL STRUCTURE OF THE TRNA SPLICING ENDONUCLEASE FROM METHANOCOCCUS JANNASCHII
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000213 | molecular_function | tRNA-intron lyase activity |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004519 | molecular_function | endonuclease activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| A | 0008033 | biological_process | tRNA processing |
| A | 0016829 | molecular_function | lyase activity |
| B | 0000213 | molecular_function | tRNA-intron lyase activity |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004519 | molecular_function | endonuclease activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| B | 0008033 | biological_process | tRNA processing |
| B | 0016829 | molecular_function | lyase activity |
| C | 0000213 | molecular_function | tRNA-intron lyase activity |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004519 | molecular_function | endonuclease activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| C | 0008033 | biological_process | tRNA processing |
| C | 0016829 | molecular_function | lyase activity |
| D | 0000213 | molecular_function | tRNA-intron lyase activity |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0004519 | molecular_function | endonuclease activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006388 | biological_process | tRNA splicing, via endonucleolytic cleavage and ligation |
| D | 0008033 | biological_process | tRNA processing |
| D | 0016829 | molecular_function | lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | TYR108 |
| A | ARG113 |
| A | TYR115 |
| A | HIS125 |
| A | SER126 |
| A | LYS156 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 2 |
| Chain | Residue |
| C | HIS125 |
| C | SER126 |
| C | LYS156 |
| C | TYR108 |
| C | ARG113 |
| C | TYR115 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU D 1 |
| Chain | Residue |
| D | CYS86 |
| D | LEU87 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU B 2 |
| Chain | Residue |
| B | CYS86 |
| B | LEU87 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU C 3 |
| Chain | Residue |
| C | TYR75 |
| C | CYS86 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU A 4 |
| Chain | Residue |
| A | TYR75 |
| A | CYS86 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9535656 |
| Chain | Residue | Details |
| A | LYS156 | |
| A | TYR115 | |
| A | HIS125 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9535656 |
| Chain | Residue | Details |
| B | LYS156 | |
| B | TYR115 | |
| B | HIS125 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9535656 |
| Chain | Residue | Details |
| C | LYS156 | |
| C | TYR115 | |
| C | HIS125 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 9535656 |
| Chain | Residue | Details |
| D | LYS156 | |
| D | TYR115 | |
| D | HIS125 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 565 |
| Chain | Residue | Details |
| A | TYR115 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | HIS125 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | LYS156 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 565 |
| Chain | Residue | Details |
| B | TYR115 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| B | HIS125 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| B | LYS156 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 565 |
| Chain | Residue | Details |
| C | TYR115 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| C | HIS125 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| C | LYS156 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 565 |
| Chain | Residue | Details |
| D | TYR115 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| D | HIS125 | increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| D | LYS156 | electrostatic stabiliser |
