6CHD
Crystal Structure of Human Lysyl-tRNA Synthetase complexed with L-Lysylsulfamoyl Adenosine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002276 | biological_process | basophil activation involved in immune response |
| A | 0002863 | biological_process | positive regulation of inflammatory response to antigenic stimulus |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004824 | molecular_function | lysine-tRNA ligase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| A | 0008033 | biological_process | tRNA processing |
| A | 0010165 | biological_process | response to X-ray |
| A | 0015966 | biological_process | diadenosine tetraphosphate biosynthetic process |
| A | 0016597 | molecular_function | amino acid binding |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043032 | biological_process | positive regulation of macrophage activation |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0070371 | biological_process | ERK1 and ERK2 cascade |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002276 | biological_process | basophil activation involved in immune response |
| B | 0002863 | biological_process | positive regulation of inflammatory response to antigenic stimulus |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003877 | molecular_function | ATP:ADP adenylyltransferase activity |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004824 | molecular_function | lysine-tRNA ligase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0008033 | biological_process | tRNA processing |
| B | 0010165 | biological_process | response to X-ray |
| B | 0015966 | biological_process | diadenosine tetraphosphate biosynthetic process |
| B | 0016597 | molecular_function | amino acid binding |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017101 | cellular_component | aminoacyl-tRNA synthetase multienzyme complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043032 | biological_process | positive regulation of macrophage activation |
| B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| B | 0070371 | biological_process | ERK1 and ERK2 cascade |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue KAA A 601 |
| Chain | Residue |
| A | GLY277 |
| A | THR337 |
| A | GLU339 |
| A | TYR341 |
| A | GLU494 |
| A | ILE495 |
| A | ASN497 |
| A | TYR499 |
| A | GLU501 |
| A | GLY546 |
| A | GLY548 |
| A | ALA299 |
| A | GLY550 |
| A | ARG553 |
| A | HOH768 |
| A | GLU301 |
| A | ARG323 |
| A | GLU325 |
| A | THR330 |
| A | HIS331 |
| A | ASN332 |
| A | PHE335 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | PRO435 |
| A | ARG442 |
| A | LYS446 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 603 |
| Chain | Residue |
| A | HIS133 |
| A | ARG148 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | LYS363 |
| A | SER368 |
| A | TYR369 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 A 605 |
| Chain | Residue |
| A | TYR383 |
| A | ASP384 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 606 |
| Chain | Residue |
| A | GLY377 |
| A | ASN562 |
| A | HOH775 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 607 |
| Chain | Residue |
| A | ILE170 |
| A | ASN174 |
| A | ARG420 |
| A | THR439 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 608 |
| Chain | Residue |
| A | PHE144 |
| A | THR191 |
| A | LYS192 |
| A | HOH791 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | binding site for residue KAA B 601 |
| Chain | Residue |
| B | GLY277 |
| B | ALA299 |
| B | GLU301 |
| B | ARG323 |
| B | GLU325 |
| B | THR330 |
| B | HIS331 |
| B | ASN332 |
| B | PHE335 |
| B | THR337 |
| B | GLU339 |
| B | TYR341 |
| B | GLU494 |
| B | ILE495 |
| B | ASN497 |
| B | TYR499 |
| B | GLU501 |
| B | GLY546 |
| B | TRP547 |
| B | GLY548 |
| B | GLY550 |
| B | ARG553 |
| B | HOH737 |
| B | HOH766 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 602 |
| Chain | Residue |
| B | ASP123 |
| B | ASP386 |
| B | THR388 |
| B | PRO390 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 603 |
| Chain | Residue |
| B | HIS331 |
| B | GLU494 |
| B | ARG553 |
| B | HOH779 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 604 |
| Chain | Residue |
| B | PRO435 |
| B | ARG442 |
| B | LYS446 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 605 |
| Chain | Residue |
| B | TYR253 |
| B | SER256 |
| B | PHE257 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 606 |
| Chain | Residue |
| B | LYS363 |
| B | HIS364 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 607 |
| Chain | Residue |
| B | HIS120 |
| B | ASN162 |
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 | GLY277 | |
| B | GLY277 |
| 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 | GLU301 | |
| B | GLU501 | |
| A | GLU339 | |
| A | TYR341 | |
| A | ASN497 | |
| A | GLU501 | |
| B | GLU301 | |
| B | GLU339 | |
| B | TYR341 | |
| B | ASN497 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18272479 |
| Chain | Residue | Details |
| A | ARG323 | |
| A | HIS331 | |
| A | GLU494 | |
| A | GLY550 | |
| B | ARG323 | |
| B | HIS331 | |
| B | GLU494 | |
| B | GLY550 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | ALA2 | |
| B | ALA2 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS88 | |
| A | LYS141 | |
| B | LYS88 | |
| B | LYS141 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539 |
| Chain | Residue | Details |
| A | SER207 | |
| B | SER207 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | SER590 | |
| A | SER596 | |
| B | SER590 | |
| B | SER596 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q99MN1 |
| Chain | Residue | Details |
| A | THR591 | |
| B | THR591 |
