2PID
Crystal structure of human mitochondrial tyrosyl-tRNA synthetase in complex with an adenylate analog
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE YSA A 384 |
| Chain | Residue |
| A | TYR77 |
| A | GLN225 |
| A | ASP228 |
| A | GLN241 |
| A | GLY243 |
| A | GLY244 |
| A | ASP246 |
| A | GLN247 |
| A | PRO272 |
| A | LEU273 |
| A | ILE274 |
| A | GLY79 |
| A | HOH388 |
| A | HOH400 |
| A | HOH403 |
| A | ASP81 |
| A | GLY90 |
| A | HIS91 |
| A | LEU111 |
| A | THR116 |
| A | ASP121 |
| A | TYR221 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE YSA B 384 |
| Chain | Residue |
| B | TYR77 |
| B | GLY79 |
| B | ASP81 |
| B | GLY90 |
| B | HIS91 |
| B | ALA94 |
| B | LEU111 |
| B | THR116 |
| B | ASP121 |
| B | TYR221 |
| B | GLN225 |
| B | ASP228 |
| B | GLN241 |
| B | GLY243 |
| B | GLY244 |
| B | ASP246 |
| B | GLN247 |
| B | PRO272 |
| B | LEU273 |
| B | ILE274 |
| B | HOH397 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHVGHL |
| Chain | Residue | Details |
| A | PRO82-LEU92 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17997975","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PID","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZXI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17997975","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PID","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BYL4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2ts1 |
| Chain | Residue | Details |
| A | ARG129 | |
| A | ARG125 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 2ts1 |
| Chain | Residue | Details |
| B | ARG129 | |
| B | ARG125 |
