1TO9
Crystal structure of THI-4 protein from Bacillus subtilis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
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 | 1901360 | biological_process | organic cyclic compound metabolic process |
B | 0005829 | cellular_component | cytosol |
B | 0006725 | biological_process | obsolete cellular aromatic compound metabolic process |
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 | 1901360 | biological_process | organic cyclic compound metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE HMH A 301 |
Chain | Residue |
A | ASP44 |
A | TYR47 |
A | ALA81 |
A | LEU85 |
A | CYS135 |
A | TYR139 |
A | TYR163 |
A | GLU205 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE HMH B 302 |
Chain | Residue |
B | TYR47 |
B | CYS135 |
B | TYR139 |
B | TYR163 |
B | GLU205 |
B | ASP44 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000303|PubMed:18054064 |
Chain | Residue | Details |
B | CYS135 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000303|PubMed:18054064 |
Chain | Residue | Details |
B | GLU205 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15709744, ECO:0000269|Ref.5 |
Chain | Residue | Details |
B | ASP44 | |
B | TYR139 | |
B | TYR163 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Increases nucleophilicity of active site Cys => ECO:0000303|PubMed:18054064 |
Chain | Residue | Details |
B | TYR47 |