3RM5
Structure of Trifunctional THI20 from Yeast
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0050334 | molecular_function | thiaminase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016740 | molecular_function | transferase 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 | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P55882","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Increases nucleophilicity of active site Cys","evidences":[{"source":"UniProtKB","id":"P25052","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
