5YZX
Crystal structure of E.coli LysU T146D mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004824 | molecular_function | lysine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| A | 0016020 | cellular_component | membrane |
| A | 0016874 | molecular_function | ligase activity |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0036260 | biological_process | RNA capping |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004824 | molecular_function | lysine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0016020 | cellular_component | membrane |
| B | 0016874 | molecular_function | ligase activity |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0036260 | biological_process | RNA capping |
| B | 0042803 | molecular_function | protein homodimerization activity |
| C | 0000049 | molecular_function | tRNA binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004824 | molecular_function | lysine-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| C | 0016020 | cellular_component | membrane |
| C | 0016874 | molecular_function | ligase activity |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0036260 | biological_process | RNA capping |
| C | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue B4P A 601 |
| Chain | Residue |
| A | ALA217 |
| A | ASP376 |
| A | GLU421 |
| A | ILE422 |
| A | ASN424 |
| A | ARG480 |
| A | ILE491 |
| A | CA602 |
| A | CA603 |
| A | CA604 |
| A | ARG262 |
| A | GLU264 |
| A | SER267 |
| A | ARG269 |
| A | HIS270 |
| A | ASN271 |
| A | PHE274 |
| A | MET276 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CA A 602 |
| Chain | Residue |
| A | GLU264 |
| A | B4P601 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 603 |
| Chain | Residue |
| A | GLU414 |
| A | GLU421 |
| A | ASN424 |
| A | B4P601 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 604 |
| Chain | Residue |
| A | ASP376 |
| A | GLU414 |
| A | GLU421 |
| A | B4P601 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue B4P B 601 |
| Chain | Residue |
| B | ARG262 |
| B | GLU264 |
| B | GLY265 |
| B | SER267 |
| B | ARG269 |
| B | HIS270 |
| B | ASN271 |
| B | PHE274 |
| B | MET276 |
| B | GLU414 |
| B | GLU421 |
| B | ILE422 |
| B | ASN424 |
| B | ARG480 |
| B | ILE491 |
| B | CA602 |
| B | CA603 |
| B | CA604 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue CA B 602 |
| Chain | Residue |
| B | GLU264 |
| B | B4P601 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue CA B 603 |
| Chain | Residue |
| B | GLU414 |
| B | GLU421 |
| B | B4P601 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CA B 604 |
| Chain | Residue |
| B | ASP376 |
| B | B4P601 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | binding site for residue B4P C 601 |
| Chain | Residue |
| C | ALA217 |
| C | ARG262 |
| C | ARG269 |
| C | HIS270 |
| C | ASN271 |
| C | PHE274 |
| C | MET276 |
| C | GLU421 |
| C | ILE422 |
| C | ASN424 |
| C | GLY477 |
| C | ARG480 |
| C | ILE491 |
| C | CA602 |
| C | CA603 |
| C | CA604 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CA C 602 |
| Chain | Residue |
| C | ASP376 |
| C | B4P601 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CA C 603 |
| Chain | Residue |
| C | GLU264 |
| C | B4P601 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue CA C 604 |
| Chain | Residue |
| C | GLU414 |
| C | GLU421 |
| C | B4P601 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
