1GAX
CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004832 | molecular_function | valine-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 | 0006438 | biological_process | valyl-tRNA aminoacylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0106074 | biological_process | aminoacyl-tRNA metabolism involved in translational fidelity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004832 | molecular_function | valine-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 | 0006438 | biological_process | valyl-tRNA aminoacylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0106074 | biological_process | aminoacyl-tRNA metabolism involved in translational fidelity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 998 |
| Chain | Residue |
| A | CYS176 |
| A | ARG178 |
| A | CYS179 |
| A | CYS344 |
| A | CYS347 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 999 |
| Chain | Residue |
| A | CYS441 |
| A | CYS417 |
| A | CYS420 |
| A | CYS438 |
| A | ALA440 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 998 |
| Chain | Residue |
| B | CYS176 |
| B | CYS179 |
| B | CYS344 |
| B | CYS347 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 999 |
| Chain | Residue |
| B | CYS417 |
| B | CYS420 |
| B | CYS438 |
| B | CYS441 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE VAA A 990 |
| Chain | Residue |
| A | PRO41 |
| A | PRO42 |
| A | ASN44 |
| A | HIS50 |
| A | GLY52 |
| A | HIS53 |
| A | ASP56 |
| A | ASP81 |
| A | SER459 |
| A | THR487 |
| A | GLY488 |
| A | ASP490 |
| A | ILE491 |
| A | TRP495 |
| A | HIS518 |
| A | GLY519 |
| A | LEU520 |
| A | VAL521 |
| A | MET529 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE VAA B 1990 |
| Chain | Residue |
| B | PRO41 |
| B | PRO42 |
| B | ASN44 |
| B | HIS50 |
| B | GLY52 |
| B | HIS53 |
| B | ASP56 |
| B | ASP81 |
| B | SER459 |
| B | THR487 |
| B | GLY488 |
| B | ASP490 |
| B | ILE491 |
| B | TRP495 |
| B | HIS518 |
| B | GLY519 |
| B | LEU520 |
| B | VAL521 |
| B | MET529 |
| B | HOH2003 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PnvTGsLHMGHA |
| Chain | Residue | Details |
| A | PRO43-ALA54 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:11114335, ECO:0000305|PubMed:12554880, ECO:0007744|PDB:1GAX, ECO:0007744|PDB:1IVS |
| Chain | Residue | Details |
| A | PRO42 | |
| A | VAL521 | |
| A | MET529 | |
| B | PRO42 | |
| B | ASN44 | |
| B | HIS50 | |
| B | HIS53 | |
| B | ASP81 | |
| B | THR487 | |
| B | GLY488 | |
| B | ASP490 | |
| A | ASN44 | |
| B | HIS518 | |
| B | VAL521 | |
| B | MET529 | |
| A | HIS50 | |
| A | HIS53 | |
| A | ASP81 | |
| A | THR487 | |
| A | GLY488 | |
| A | ASP490 | |
| A | HIS518 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS176 | |
| B | CYS179 | |
| B | CYS344 | |
| B | CYS347 | |
| B | CYS417 | |
| B | CYS420 | |
| B | CYS438 | |
| B | CYS441 | |
| A | CYS179 | |
| A | CYS344 | |
| A | CYS347 | |
| A | CYS417 | |
| A | CYS420 | |
| A | CYS438 | |
| A | CYS441 | |
| B | CYS176 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS531 | |
| B | LYS531 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Interaction with tRNA |
| Chain | Residue | Details |
| A | ARG570 | |
| B | ARG570 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a8h |
| Chain | Residue | Details |
| A | LYS528 | |
| A | LYS531 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a8h |
| Chain | Residue | Details |
| B | LYS528 | |
| B | LYS531 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1a8h |
| Chain | Residue | Details |
| B | LYS531 |
