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 endonuclease activity |
A | 0000379 | biological_process | tRNA-type intron splice site recognition and cleavage |
A | 0003676 | molecular_function | nucleic acid binding |
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 endonuclease activity |
B | 0000379 | biological_process | tRNA-type intron splice site recognition and cleavage |
B | 0003676 | molecular_function | nucleic acid binding |
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 endonuclease activity |
C | 0000379 | biological_process | tRNA-type intron splice site recognition and cleavage |
C | 0003676 | molecular_function | nucleic acid binding |
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 endonuclease activity |
D | 0000379 | biological_process | tRNA-type intron splice site recognition and cleavage |
D | 0003676 | molecular_function | nucleic acid binding |
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 | ACT_SITE: |
Chain | Residue | Details |
A | TYR115 | |
D | TYR115 | |
D | HIS125 | |
D | LYS156 | |
A | HIS125 | |
A | LYS156 | |
B | TYR115 | |
B | HIS125 | |
B | LYS156 | |
C | TYR115 | |
C | HIS125 | |
C | LYS156 |
Catalytic Information from CSA
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 |