3RM5
Structure of Trifunctional THI20 from Yeast
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006772 | biological_process | thiamine metabolic process |
A | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
A | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0009230 | biological_process | thiamine catabolic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0050334 | molecular_function | thiaminase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006772 | biological_process | thiamine metabolic process |
B | 0008902 | molecular_function | hydroxymethylpyrimidine kinase activity |
B | 0008972 | molecular_function | phosphomethylpyrimidine kinase activity |
B | 0009228 | biological_process | thiamine biosynthetic process |
B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
B | 0009230 | biological_process | thiamine catabolic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0050334 | molecular_function | thiaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 1 |
Chain | Residue |
A | ASP126 |
A | PRO127 |
A | VAL128 |
A | THR158 |
A | ASN160 |
A | GLU163 |
A | LYS199 |
A | GLY242 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 552 |
Chain | Residue |
A | GLN525 |
A | HOH590 |
B | TYR14 |
A | GLU302 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 552 |
Chain | Residue |
A | TYR295 |
B | PRO12 |
B | GLU298 |
B | PRO300 |
B | LYS303 |
B | MET304 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250|UniProtKB:P25052 |
Chain | Residue | Details |
A | CYS468 | |
B | CYS468 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P25052 |
Chain | Residue | Details |
A | GLU540 | |
B | GLU540 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P55882 |
Chain | Residue | Details |
A | GLN64 | |
B | GLN64 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Increases nucleophilicity of active site Cys => ECO:0000250|UniProtKB:P25052 |
Chain | Residue | Details |
A | TYR379 | |
B | TYR379 |