1JZQ
Isoleucyl-tRNA synthetase Complexed with Isoleucyl-adenylate analogue
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002161 | molecular_function | aminoacyl-tRNA deacylase activity |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004822 | molecular_function | isoleucine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006428 | biological_process | isoleucyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1101 |
| Chain | Residue |
| A | CYS181 |
| A | CYS184 |
| A | CYS389 |
| A | CYS392 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1102 |
| Chain | Residue |
| A | CYS461 |
| A | CYS464 |
| A | GLY465 |
| A | CYS502 |
| A | CYS504 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ILA A 1301 |
| Chain | Residue |
| A | GLY45 |
| A | PRO46 |
| A | HIS54 |
| A | GLY56 |
| A | HIS57 |
| A | GLN59 |
| A | ASP85 |
| A | GLU550 |
| A | GLY551 |
| A | ASP553 |
| A | GLN554 |
| A | TRP558 |
| A | HIS581 |
| A | GLY582 |
| A | LEU583 |
| A | ILE584 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PtaNGlPHVGHA |
| Chain | Residue | Details |
| A | PRO47-ALA58 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Motif: {"description":"'HIGH' region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11584022","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1JZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1ILE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JZQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JZS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14672940","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1ILE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1JZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1ILE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a8h |
| Chain | Residue | Details |
| A | LYS591 | |
| A | LYS594 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 309 |
| Chain | Residue | Details |
| A | PRO46 | steric role, van der waals interaction |
| A | ASP85 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, steric role |
| A | TRP518 | steric role, van der waals interaction |
| A | GLN554 | hydrogen bond acceptor, steric role |
| A | TRP558 | steric role, van der waals interaction |
| A | LYS591 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| A | LYS594 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
