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 site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23159739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19524539","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
