1Q4T
crystal structure of 4-hydroxybenzoyl CoA thioesterase from Arthrobacter sp. strain SU complexed with 4-hydroxyphenyl 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 | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 152 |
| Chain | Residue |
| B | ARG115 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 152 |
| Chain | Residue |
| A | ARG115 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL A 153 |
| Chain | Residue |
| A | ALA10 |
| A | THR11 |
| A | GLY12 |
| A | GLY13 |
| A | ASN14 |
| A | LEU15 |
| A | HOH422 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 153 |
| Chain | Residue |
| B | GLY12 |
| B | GLY13 |
| B | ASN14 |
| B | LEU15 |
| B | TYR26 |
| site_id | AC5 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE 4CO A 370 |
| Chain | Residue |
| A | LEU15 |
| A | GLU73 |
| A | MET74 |
| A | THR77 |
| A | GLU78 |
| A | MET90 |
| A | GLY93 |
| A | HIS117 |
| A | GLY119 |
| A | SER120 |
| A | THR121 |
| A | THR122 |
| A | ARG147 |
| A | PRO148 |
| A | ARG150 |
| A | HOH375 |
| A | HOH376 |
| A | HOH402 |
| A | HOH403 |
| A | HOH419 |
| A | HOH420 |
| A | HOH499 |
| A | HOH500 |
| B | GLN58 |
| B | VAL63 |
| B | HIS64 |
| B | GLY65 |
| B | PHE100 |
| B | PHE101 |
| B | ARG102 |
| B | PRO103 |
| B | HOH401 |
| B | HOH412 |
| site_id | AC6 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE 4CO B 371 |
| Chain | Residue |
| A | GLN58 |
| A | VAL63 |
| A | HIS64 |
| A | GLY65 |
| A | PHE100 |
| A | PHE101 |
| A | ARG102 |
| A | PRO103 |
| A | HOH400 |
| B | LEU15 |
| B | GLU73 |
| 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 | HOH383 |
| B | HOH403 |
| B | HOH407 |
| B | HOH428 |
| B | HOH429 |
| B | HOH432 |
| B | HOH497 |
| B | HOH502 |
| B | HOH516 |
| B | HOH517 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 371 |
| Chain | Residue |
| A | VAL81 |
| A | MET89 |
| A | MET90 |
| A | ALA91 |
| A | HOH454 |
| B | TRP60 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 372 |
| Chain | Residue |
| B | VAL18 |
| B | ALA19 |
| B | SER20 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 373 |
| Chain | Residue |
| A | TRP60 |
| B | VAL81 |
| B | MET90 |
| B | ALA91 |
| B | HOH430 |
| B | HOH440 |
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 |
| B | GLU73 | |
| A | GLU73 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE100 | |
| B | PHE100 |
