3R35
Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase mutant E73D complexed with 4-hydroxyphenacyl CoA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0018739 | molecular_function | 4-hydroxybenzoyl-CoA thioesterase activity |
| A | 0042372 | biological_process | phylloquinone biosynthetic process |
| A | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016289 | molecular_function | acyl-CoA hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0018739 | molecular_function | 4-hydroxybenzoyl-CoA thioesterase activity |
| B | 0042372 | biological_process | phylloquinone biosynthetic process |
| B | 0061522 | molecular_function | 1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE 4CO A 170 |
| Chain | Residue |
| A | LEU15 |
| A | GLY119 |
| A | SER120 |
| A | THR121 |
| A | THR122 |
| A | ARG147 |
| A | PRO148 |
| A | ARG150 |
| A | HOH509 |
| A | HOH524 |
| A | HOH543 |
| A | ASP73 |
| A | HOH626 |
| A | HOH800 |
| A | HOH868 |
| B | GLN58 |
| B | HIS64 |
| B | GLY65 |
| B | PHE100 |
| B | PHE101 |
| B | ARG102 |
| B | PRO103 |
| A | MET74 |
| B | HOH500 |
| A | THR77 |
| A | GLU78 |
| A | MET90 |
| A | VAL92 |
| A | GLY93 |
| A | HIS117 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE 4CO B 170 |
| Chain | Residue |
| A | GLN58 |
| A | HIS64 |
| A | GLY65 |
| A | PHE100 |
| A | PHE101 |
| A | ARG102 |
| A | PRO103 |
| A | HOH501 |
| A | HOH506 |
| B | LEU15 |
| B | ASP73 |
| B | MET74 |
| B | THR77 |
| B | GLU78 |
| B | MET90 |
| B | GLY93 |
| B | HIS117 |
| B | GLY119 |
| B | SER120 |
| B | THR121 |
| B | THR122 |
| B | ARG147 |
| B | PRO148 |
| B | ARG150 |
| B | HOH504 |
| B | HOH507 |
| B | HOH547 |
| B | HOH579 |
| B | HOH654 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:12907670 |
| Chain | Residue | Details |
| A | ASP73 | |
| B | ASP73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE100 | |
| B | PHE100 |
