2X1L
Crystal structure of Mycobacterium smegmatis methionyl-tRNA synthetase in complex with methionine and adenosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004825 | molecular_function | methionine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006431 | biological_process | methionyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004825 | molecular_function | methionine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006431 | biological_process | methionyl-tRNA aminoacylation |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004825 | molecular_function | methionine-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006431 | biological_process | methionyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE MET A 600 |
Chain | Residue |
A | ILE11 |
A | HIS270 |
A | ADN601 |
A | HOH2169 |
A | HOH2170 |
A | HOH2171 |
A | ALA12 |
A | TYR13 |
A | ASP50 |
A | TRP230 |
A | ALA233 |
A | LEU234 |
A | TYR237 |
A | ILE266 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN A 601 |
Chain | Residue |
A | ALA10 |
A | ALA12 |
A | HIS19 |
A | GLY21 |
A | HIS22 |
A | GLU25 |
A | GLY263 |
A | ASP265 |
A | ILE266 |
A | HIS292 |
A | GLY293 |
A | TRP294 |
A | LEU295 |
A | MET600 |
A | HOH2171 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CXS A 602 |
Chain | Residue |
A | ALA114 |
A | GLY115 |
A | ASP116 |
A | ALA170 |
A | TYR171 |
A | ARG174 |
A | HOH2172 |
B | TYR452 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 2HP A 603 |
Chain | Residue |
A | PRO188 |
A | ASP189 |
A | ARG288 |
A | VAL406 |
A | HOH2082 |
A | HOH2173 |
A | HOH2174 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MET B 600 |
Chain | Residue |
B | ILE11 |
B | TYR13 |
B | ASP50 |
B | TRP230 |
B | ALA233 |
B | TYR237 |
B | ILE266 |
B | HIS270 |
B | ADN601 |
B | HOH2140 |
B | HOH2141 |
B | HOH2142 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN B 601 |
Chain | Residue |
B | ALA10 |
B | HIS19 |
B | GLY21 |
B | HIS22 |
B | GLU25 |
B | GLY263 |
B | ASP265 |
B | ILE266 |
B | HIS292 |
B | GLY293 |
B | TRP294 |
B | LEU295 |
B | MET600 |
B | HOH2140 |
B | HOH2143 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CXS B 602 |
Chain | Residue |
B | ALA114 |
B | GLY115 |
B | ASP116 |
B | ALA170 |
B | TYR171 |
B | ARG174 |
B | HOH2055 |
C | TYR452 |
C | ARG495 |
C | HOH2119 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 2HP B 603 |
Chain | Residue |
B | GLY187 |
B | PRO188 |
B | ASP189 |
B | ARG288 |
B | VAL406 |
B | HOH2146 |
B | HOH2147 |
B | HOH2148 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE MET C 600 |
Chain | Residue |
C | HOH2158 |
C | ILE11 |
C | TYR13 |
C | ASP50 |
C | TRP230 |
C | ALA233 |
C | TYR237 |
C | ILE266 |
C | HIS270 |
C | ADN601 |
C | HOH2156 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADN C 601 |
Chain | Residue |
C | ALA10 |
C | ALA12 |
C | HIS19 |
C | GLY21 |
C | HIS22 |
C | GLU25 |
C | GLY263 |
C | ASP265 |
C | ILE266 |
C | HIS292 |
C | GLY293 |
C | TRP294 |
C | LEU295 |
C | MET600 |
C | HOH2004 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CXS C 602 |
Chain | Residue |
A | TYR452 |
A | ARG495 |
C | ALA114 |
C | ASP116 |
C | ALA170 |
C | TYR171 |
C | ARG174 |
C | HOH2159 |
C | HOH2160 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 2HP C 603 |
Chain | Residue |
C | GLY187 |
C | PRO188 |
C | ASP189 |
C | ARG288 |
C | VAL406 |
C | HOH2068 |
C | HOH2161 |
C | HOH2162 |
Functional Information from PROSITE/UniProt
site_id | PS00178 |
Number of Residues | 10 |
Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..NGvPHIGHA |
Chain | Residue | Details |
A | PRO14-ALA23 |