1KMN
HISTIDYL-TRNA SYNTHETASE COMPLEXED WITH HISTIDINOL AND ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004821 | molecular_function | histidine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0140101 | molecular_function | catalytic activity, acting on a tRNA |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004821 | molecular_function | histidine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0140101 | molecular_function | catalytic activity, acting on a tRNA |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004821 | molecular_function | histidine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006412 | biological_process | translation |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| C | 0016874 | molecular_function | ligase activity |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0140101 | molecular_function | catalytic activity, acting on a tRNA |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| D | 0004821 | molecular_function | histidine-tRNA ligase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006412 | biological_process | translation |
| D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| D | 0006427 | biological_process | histidyl-tRNA aminoacylation |
| D | 0016874 | molecular_function | ligase activity |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0140101 | molecular_function | catalytic activity, acting on a tRNA |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HSO A 451 |
| Chain | Residue |
| A | GLU83 |
| A | THR85 |
| A | GLN127 |
| A | GLU131 |
| A | TYR263 |
| A | TYR264 |
| A | GLY286 |
| A | TYR288 |
| A | GLY304 |
| A | PHE305 |
| A | ATP452 |
| A | HOH519 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ATP A 452 |
| Chain | Residue |
| A | ARG113 |
| A | GLU115 |
| A | GLY120 |
| A | ARG121 |
| A | TYR122 |
| A | PHE125 |
| A | GLN127 |
| A | ARG259 |
| A | THR281 |
| A | VAL282 |
| A | GLY308 |
| A | ARG311 |
| A | HSO451 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HSO B 451 |
| Chain | Residue |
| B | THR85 |
| B | TYR107 |
| B | GLN127 |
| B | GLU131 |
| B | TYR263 |
| B | TYR264 |
| B | TYR288 |
| B | GLY304 |
| B | PHE305 |
| B | ALA306 |
| B | ATP452 |
| B | GLU83 |
| B | GLY84 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP B 452 |
| Chain | Residue |
| B | ARG113 |
| B | GLU115 |
| B | GLY120 |
| B | ARG121 |
| B | TYR122 |
| B | PHE125 |
| B | GLN127 |
| B | ARG259 |
| B | THR281 |
| B | VAL282 |
| B | ALA284 |
| B | ALA306 |
| B | GLY308 |
| B | ARG311 |
| B | HSO451 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HSO C 451 |
| Chain | Residue |
| C | GLU83 |
| C | THR85 |
| C | GLN127 |
| C | GLU131 |
| C | TYR263 |
| C | TYR264 |
| C | GLY285 |
| C | TYR288 |
| C | GLY304 |
| C | ATP452 |
| C | HOH501 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP C 452 |
| Chain | Residue |
| C | ARG113 |
| C | GLY120 |
| C | TYR122 |
| C | PHE125 |
| C | GLN127 |
| C | ARG259 |
| C | THR281 |
| C | VAL282 |
| C | GLY308 |
| C | ARG311 |
| C | HSO451 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HSO D 451 |
| Chain | Residue |
| D | GLU83 |
| D | THR85 |
| D | GLN127 |
| D | GLU131 |
| D | TYR263 |
| D | TYR264 |
| D | TYR288 |
| D | GLY304 |
| D | PHE305 |
| D | ALA306 |
| D | ATP452 |
| D | HOH503 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ATP D 452 |
| Chain | Residue |
| D | ARG113 |
| D | GLU115 |
| D | GLY120 |
| D | ARG121 |
| D | TYR122 |
| D | PHE125 |
| D | GLN127 |
| D | ARG259 |
| D | THR281 |
| D | VAL282 |
| D | ALA284 |
| D | ALA306 |
| D | GLY308 |
| D | ARG311 |
| D | HSO451 |
| site_id | S1A |
| Number of Residues | 18 |
| Details | HISTIDINE AND ATP BINDING SITE, SUBSTRATES OF THE FIRST REACTION: HISTIDINOL (AN INHIBITOR) AND ATP (BOTH OBSERVED IN THE SITE). |
| Chain | Residue |
| A | GLU83 |
| A | ARG259 |
| A | TYR263 |
| A | TYR264 |
| A | GLU270 |
| A | THR281 |
| A | TYR288 |
| A | ARG311 |
| A | HSO451 |
| A | ATP452 |
| A | THR85 |
| A | ARG113 |
| A | GLU115 |
| A | ARG121 |
| A | TYR122 |
| A | PHE125 |
| A | GLN127 |
| A | GLU131 |
| site_id | S1B |
| Number of Residues | 18 |
| Details | HISTIDINE AND ATP BINDING SITE, SUBSTRATES OF THE FIRST REACTION: HISTIDINOL (AN INHIBITOR) AND ATP (BOTH OBSERVED IN THE SITE). |
| Chain | Residue |
| B | GLU83 |
| B | THR85 |
| B | ARG113 |
| B | GLU115 |
| B | ARG121 |
| B | TYR122 |
| B | PHE125 |
| B | GLN127 |
| B | GLU131 |
| B | ARG259 |
| B | TYR263 |
| B | TYR264 |
| B | GLU270 |
| B | THR281 |
| B | TYR288 |
| B | ARG311 |
| B | HSO451 |
| B | ATP452 |
| site_id | S1C |
| Number of Residues | 18 |
| Details | HISTIDINE AND ATP BINDING SITE, SUBSTRATES OF THE FIRST REACTION: HISTIDINOL (AN INHIBITOR) AND ATP (BOTH OBSERVED IN THE SITE). |
| Chain | Residue |
| C | GLU83 |
| C | THR85 |
| C | ARG113 |
| C | GLU115 |
| C | ARG121 |
| C | TYR122 |
| C | PHE125 |
| C | GLN127 |
| C | GLU131 |
| C | ARG259 |
| C | TYR263 |
| C | TYR264 |
| C | GLU270 |
| C | THR281 |
| C | TYR288 |
| C | ARG311 |
| C | HSO451 |
| C | ATP452 |
| site_id | S1D |
| Number of Residues | 18 |
| Details | HISTIDINE AND ATP BINDING SITE, SUBSTRATES OF THE FIRST REACTION: HISTIDINOL (AN INHIBITOR) AND ATP (BOTH OBSERVED IN THE SITE). |
| Chain | Residue |
| D | GLU83 |
| D | THR85 |
| D | ARG113 |
| D | GLU115 |
| D | ARG121 |
| D | TYR122 |
| D | PHE125 |
| D | GLN127 |
| D | GLU131 |
| D | ARG259 |
| D | TYR263 |
| D | TYR264 |
| D | GLU270 |
| D | THR281 |
| D | TYR288 |
| D | ARG311 |
| D | HSO451 |
| D | ATP452 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| A | ARG113 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| B | ARG113 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| C | ARG113 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1qf6 |
| Chain | Residue | Details |
| D | ARG113 |
