1H4T
Prolyl-tRNA synthetase from Thermus thermophilus complexed with L-proline
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004827 | molecular_function | proline-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006433 | biological_process | prolyl-tRNA aminoacylation |
A | 0046872 | molecular_function | metal ion binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004827 | molecular_function | proline-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006433 | biological_process | prolyl-tRNA aminoacylation |
B | 0046872 | molecular_function | metal ion binding |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004827 | molecular_function | proline-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006433 | biological_process | prolyl-tRNA aminoacylation |
C | 0046872 | molecular_function | metal ion binding |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
D | 0004827 | molecular_function | proline-tRNA ligase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006412 | biological_process | translation |
D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
D | 0006433 | biological_process | prolyl-tRNA aminoacylation |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 490 |
Chain | Residue |
A | CYS427 |
A | CYS432 |
A | CYS458 |
A | CYS461 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 490 |
Chain | Residue |
B | CYS427 |
B | CYS432 |
B | CYS458 |
B | CYS461 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 490 |
Chain | Residue |
C | CYS432 |
C | CYS458 |
C | CYS461 |
C | CYS427 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN D 490 |
Chain | Residue |
D | CYS427 |
D | CYS432 |
D | CYS458 |
D | CYS461 |
site_id | AC5 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PRO A1478 |
Chain | Residue |
A | THR111 |
A | GLU113 |
A | ARG142 |
A | TRP158 |
A | GLU160 |
A | PHE205 |
A | HIS230 |
A | SER258 |
A | TRP259 |
A | GLY260 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PRO B1478 |
Chain | Residue |
B | THR111 |
B | GLU113 |
B | ARG142 |
B | TRP158 |
B | GLU160 |
B | PHE205 |
B | THR228 |
B | HIS230 |
B | SER258 |
B | TRP259 |
B | GLY260 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PRO C1478 |
Chain | Residue |
C | THR111 |
C | GLU113 |
C | ARG142 |
C | TRP158 |
C | GLU160 |
C | PHE205 |
C | THR228 |
C | HIS230 |
C | SER258 |
C | TRP259 |
C | GLY260 |
C | HOH2112 |
site_id | AC8 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PRO D1478 |
Chain | Residue |
D | THR111 |
D | GLU113 |
D | ARG142 |
D | TRP158 |
D | GLU160 |
D | PHE205 |
D | THR228 |
D | HIS230 |
D | SER258 |
D | TRP259 |
D | GLY260 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11399074 |
Chain | Residue | Details |
A | THR111 | |
C | GLU113 | |
C | ARG142 | |
C | HIS230 | |
D | THR111 | |
D | GLU113 | |
D | ARG142 | |
D | HIS230 | |
A | GLU113 | |
A | ARG142 | |
A | HIS230 | |
B | THR111 | |
B | GLU113 | |
B | ARG142 | |
B | HIS230 | |
C | THR111 |
site_id | SWS_FT_FI2 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000305|PubMed:11399074 |
Chain | Residue | Details |
A | THR153 | |
B | ARG264 | |
C | THR153 | |
C | GLN225 | |
C | THR228 | |
C | SER262 | |
C | ARG264 | |
D | THR153 | |
D | GLN225 | |
D | THR228 | |
D | SER262 | |
A | GLN225 | |
D | ARG264 | |
A | THR228 | |
A | SER262 | |
A | ARG264 | |
B | THR153 | |
B | GLN225 | |
B | THR228 | |
B | SER262 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10970866, ECO:0000269|PubMed:11399074 |
Chain | Residue | Details |
A | CYS427 | |
C | CYS432 | |
C | CYS458 | |
C | CYS461 | |
D | CYS427 | |
D | CYS432 | |
D | CYS458 | |
D | CYS461 | |
A | CYS432 | |
A | CYS458 | |
A | CYS461 | |
B | CYS427 | |
B | CYS432 | |
B | CYS458 | |
B | CYS461 | |
C | CYS427 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
A | ARG142 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
B | ARG142 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
C | ARG142 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1qf6 |
Chain | Residue | Details |
D | ARG142 |