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 |