4YCU
Crystal structure of cladosporin in complex with human lysyl-tRNA synthetase
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue KRS A 601 |
| Chain | Residue |
| A | ARG323 |
| A | ARG553 |
| A | LYS602 |
| A | HOH757 |
| A | HOH863 |
| A | GLU325 |
| A | HIS331 |
| A | ASN332 |
| A | PHE335 |
| A | THR337 |
| A | GLU494 |
| A | ILE495 |
| A | GLY550 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue LYS A 602 |
| Chain | Residue |
| A | GLY277 |
| A | GLU301 |
| A | ARG323 |
| A | GLU339 |
| A | TYR341 |
| A | ASN497 |
| A | TYR499 |
| A | GLU501 |
| A | GLY546 |
| A | GLY548 |
| A | KRS601 |
| A | HOH748 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 603 |
| Chain | Residue |
| A | ARG131 |
| A | HIS133 |
| A | GLY149 |
| A | GLU150 |
| A | GLY151 |
| A | ILE235 |
| A | ARG241 |
| A | HOH803 |
| A | HOH872 |
| A | HOH919 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 604 |
| Chain | Residue |
| A | ASP445 |
| A | GLU453 |
| A | GLU487 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue KRS B 601 |
| Chain | Residue |
| B | ARG323 |
| B | GLU325 |
| B | HIS331 |
| B | ASN332 |
| B | PHE335 |
| B | THR337 |
| B | GLU494 |
| B | ILE495 |
| B | CYS496 |
| B | GLY550 |
| B | ARG553 |
| B | LYS602 |
| B | HOH826 |
| B | HOH896 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue LYS B 602 |
| Chain | Residue |
| B | GLY277 |
| B | GLU301 |
| B | ARG323 |
| B | GLU339 |
| B | TYR341 |
| B | ASN497 |
| B | TYR499 |
| B | GLU501 |
| B | GLY546 |
| B | KRS601 |
| B | HOH760 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 603 |
| Chain | Residue |
| B | TYR347 |
| B | MET351 |
| B | ARG393 |
| B | ASN395 |
| B | CYS463 |
| B | ASP464 |
| B | HOH852 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 604 |
| Chain | Residue |
| B | ASP445 |
| B | GLU453 |
| B | GLU487 |
| B | GLU494 |
| B | HOH739 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | LYS249 | |
| B | LYS249 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:26074468 |
| Chain | Residue | Details |
| A | ILE273 | |
| B | ALA473 | |
| A | GLY311 | |
| A | ASP313 | |
| A | MET469 | |
| A | ALA473 | |
| B | ILE273 | |
| B | GLY311 | |
| B | ASP313 | |
| B | MET469 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479 |
| Chain | Residue | Details |
| A | TYR295 | |
| A | TYR303 | |
| A | PRO466 | |
| A | GLY522 | |
| B | TYR295 | |
| B | TYR303 | |
| B | PRO466 | |
| B | GLY522 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | SER113 | |
| B | SER113 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539 |
| Chain | Residue | Details |
| A | GLY179 | |
| B | GLY179 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | ASN562 | |
| A | LEU568 | |
| B | ASN562 | |
| B | LEU568 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | ASN563 | |
| B | ASN563 |
