3QH2
Crystal structure of TenI from Bacillus subtilis complexed with product cThz-P
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009228 | biological_process | thiamine biosynthetic process |
A | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
A | 0016853 | molecular_function | isomerase activity |
B | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009228 | biological_process | thiamine biosynthetic process |
B | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
B | 0016853 | molecular_function | isomerase activity |
C | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0009228 | biological_process | thiamine biosynthetic process |
C | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
C | 0016853 | molecular_function | isomerase activity |
D | 0004789 | molecular_function | thiamine-phosphate diphosphorylase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0009228 | biological_process | thiamine biosynthetic process |
D | 0009229 | biological_process | thiamine diphosphate biosynthetic process |
D | 0016853 | molecular_function | isomerase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 3NM A 900 |
Chain | Residue |
A | ARG33 |
A | HOH222 |
A | HOH231 |
A | HOH264 |
A | HOH270 |
A | HIS102 |
A | GLY121 |
A | HIS122 |
A | ILE154 |
A | GLY156 |
A | MET176 |
A | SER177 |
A | HOH206 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 901 |
Chain | Residue |
A | ARG35 |
A | GLY63 |
A | HOH219 |
B | SER38 |
B | ALA39 |
B | ARG64 |
B | HOH209 |
B | HOH253 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 3NM B 900 |
Chain | Residue |
B | ARG33 |
B | HIS102 |
B | GLY121 |
B | HIS122 |
B | ILE154 |
B | GLY156 |
B | MET176 |
B | SER177 |
B | HOH206 |
B | HOH216 |
B | HOH217 |
B | HOH232 |
B | HOH241 |
B | HOH248 |
B | HOH265 |
B | HOH266 |
site_id | AC4 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 3NM C 900 |
Chain | Residue |
C | ARG33 |
C | HIS102 |
C | GLY121 |
C | HIS122 |
C | ILE154 |
C | GLY156 |
C | MET176 |
C | SER177 |
C | HOH207 |
C | HOH210 |
C | HOH220 |
C | HOH225 |
C | HOH265 |
C | HOH276 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 3NM D 900 |
Chain | Residue |
D | ARG33 |
D | HIS102 |
D | GLY121 |
D | HIS122 |
D | ILE154 |
D | GLY156 |
D | MET176 |
D | SER177 |
D | HOH207 |
D | HOH214 |
D | HOH218 |
D | HOH224 |
D | HOH258 |
D | HOH279 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000303|PubMed:21534620 |
Chain | Residue | Details |
A | HIS122 | |
B | HIS122 | |
C | HIS122 | |
D | HIS122 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21534620 |
Chain | Residue | Details |
A | HIS102 | |
D | HIS102 | |
D | GLY156 | |
D | MET176 | |
A | GLY156 | |
A | MET176 | |
B | HIS102 | |
B | GLY156 | |
B | MET176 | |
C | HIS102 | |
C | GLY156 | |
C | MET176 |