4YCW
Crystal structure of cladosporin in complex with plasmodium like human lysyl-tRNA synthetase mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide 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 | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide 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 | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| C | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| D | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| E | 0004824 | molecular_function | lysine-tRNA ligase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| E | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| F | 0004824 | molecular_function | lysine-tRNA ligase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| F | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| G | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| H | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue KRS A 602 |
| Chain | Residue |
| A | ARG323 |
| A | GLY550 |
| A | ARG553 |
| A | GLU325 |
| A | HIS331 |
| A | ASN332 |
| A | PHE335 |
| A | GLU494 |
| A | ILE495 |
| A | CYS496 |
| A | ASN497 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue KRS B 602 |
| Chain | Residue |
| B | ARG323 |
| B | GLU325 |
| B | THR330 |
| B | HIS331 |
| B | ASN332 |
| B | PHE335 |
| B | GLU494 |
| B | ILE495 |
| B | CYS496 |
| B | ASN497 |
| B | GLY550 |
| B | ARG553 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue KRS E 602 |
| Chain | Residue |
| E | GLU325 |
| E | ASN332 |
| E | PHE335 |
| E | SER337 |
| E | ASN497 |
| E | GLY550 |
| E | ARG553 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue KRS F 602 |
| Chain | Residue |
| F | ARG323 |
| F | GLU325 |
| F | HIS331 |
| F | ASN332 |
| F | PHE335 |
| F | SER337 |
| F | ILE495 |
| F | CYS496 |
| F | ASN497 |
| F | GLY550 |
| F | ARG553 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | LYS249 | |
| B | LYS249 | |
| E | LYS249 | |
| F | LYS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | ILE273 | |
| B | ALA473 | |
| E | ILE273 | |
| E | GLY311 | |
| E | ASP313 | |
| E | MET469 | |
| E | ALA473 | |
| F | ILE273 | |
| F | GLY311 | |
| F | ASP313 | |
| F | MET469 | |
| A | GLY311 | |
| F | ALA473 | |
| A | ASP313 | |
| A | MET469 | |
| A | ALA473 | |
| B | ILE273 | |
| B | GLY311 | |
| B | ASP313 | |
| B | MET469 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479 |
| Chain | Residue | Details |
| A | TYR295 | |
| E | TYR303 | |
| E | PRO466 | |
| E | GLY522 | |
| F | TYR295 | |
| F | TYR303 | |
| F | PRO466 | |
| F | GLY522 | |
| A | TYR303 | |
| A | PRO466 | |
| A | GLY522 | |
| B | TYR295 | |
| B | TYR303 | |
| B | PRO466 | |
| B | GLY522 | |
| E | TYR295 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | SER113 | |
| B | SER113 | |
| E | SER113 | |
| F | SER113 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539 |
| Chain | Residue | Details |
| A | GLY179 | |
| B | GLY179 | |
| E | GLY179 | |
| F | GLY179 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | ASN562 | |
| A | LEU568 | |
| B | ASN562 | |
| B | LEU568 | |
| E | ASN562 | |
| E | LEU568 | |
| F | ASN562 | |
| F | LEU568 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | ASN563 | |
| B | ASN563 | |
| E | ASN563 | |
| F | ASN563 |
