3R3A
Crystal structure of Arthrobacter sp. strain SU 4-hydroxybenzoyl CoA thioesterase mutant Q58A complexed with 4-hydroxybenzoic acid and 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 | 19 |
Details | BINDING SITE FOR RESIDUE COA A 170 |
Chain | Residue |
A | MET90 |
A | ARG150 |
A | PHB171 |
A | HOH619 |
A | HOH719 |
A | HOH724 |
B | VAL63 |
B | PHE100 |
B | PHE101 |
B | ARG102 |
B | PRO103 |
A | GLY93 |
A | HIS117 |
A | GLY119 |
A | SER120 |
A | THR121 |
A | THR122 |
A | ARG147 |
A | PRO148 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PHB A 171 |
Chain | Residue |
A | LEU15 |
A | GLU73 |
A | MET74 |
A | THR77 |
A | GLU78 |
A | VAL92 |
A | GLY93 |
A | COA170 |
A | HOH640 |
B | ALA58 |
B | TRP60 |
B | HIS64 |
B | GLY65 |
site_id | AC3 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE COA A 152 |
Chain | Residue |
A | VAL63 |
A | PHE100 |
A | PHE101 |
A | ARG102 |
A | PRO103 |
A | HOH604 |
A | HOH699 |
A | HOH741 |
A | HOH1083 |
A | HOH1139 |
B | MET90 |
B | GLY93 |
B | HIS117 |
B | GLY119 |
B | SER120 |
B | THR121 |
B | THR122 |
B | ARG147 |
B | PRO148 |
B | ARG150 |
B | PHB171 |
B | HOH753 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PHB B 171 |
Chain | Residue |
A | ALA58 |
A | TRP60 |
A | HIS64 |
A | GLY65 |
A | COA152 |
B | LEU15 |
B | GLU73 |
B | MET74 |
B | THR77 |
B | GLU78 |
B | GLY93 |
B | HOH605 |
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 | GLU73 | |
B | GLU73 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | PHE100 | |
B | PHE100 |