2QCX
Crystal structure of Bacillus subtilis TenA Y112F mutant complexed with formyl aminomethyl pyrimidine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006772 | biological_process | thiamine metabolic process |
| A | 0006790 | biological_process | sulfur compound metabolic process |
| A | 0009228 | biological_process | thiamine biosynthetic process |
| A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0050334 | molecular_function | thiaminase activity |
| A | 0072527 | biological_process | pyrimidine-containing compound metabolic process |
| A | 1901615 | biological_process | organic hydroxy compound metabolic process |
| B | 0005829 | cellular_component | cytosol |
| B | 0006772 | biological_process | thiamine metabolic process |
| B | 0006790 | biological_process | sulfur compound metabolic process |
| B | 0009228 | biological_process | thiamine biosynthetic process |
| B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0050334 | molecular_function | thiaminase activity |
| B | 0072527 | biological_process | pyrimidine-containing compound metabolic process |
| B | 1901615 | biological_process | organic hydroxy compound metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PF1 A 300 |
| Chain | Residue |
| A | ASP44 |
| A | GLU205 |
| A | HOH317 |
| A | TYR47 |
| A | LEU48 |
| A | PHE51 |
| A | CYS135 |
| A | TYR136 |
| A | TYR139 |
| A | TYR163 |
| A | PHE168 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PF1 B 300 |
| Chain | Residue |
| B | ASP44 |
| B | TYR47 |
| B | LEU48 |
| B | PHE51 |
| B | CYS135 |
| B | TYR136 |
| B | TYR139 |
| B | TYR163 |
| B | GLU205 |
| B | PHE208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000303|PubMed:18054064 |
| Chain | Residue | Details |
| A | CYS135 | |
| B | CYS135 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000303|PubMed:18054064 |
| Chain | Residue | Details |
| A | GLU205 | |
| B | GLU205 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5 |
| Chain | Residue | Details |
| A | ASP44 | |
| A | TYR139 | |
| A | TYR163 | |
| B | ASP44 | |
| B | TYR139 | |
| B | TYR163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Increases nucleophilicity of active site Cys => ECO:0000303|PubMed:18054064 |
| Chain | Residue | Details |
| A | TYR47 | |
| B | TYR47 |
