6PI1
Crystal structure of Marinobacter subterrani acetylpolyamine amidohydrolase (msAPAH) complexed with 4-(dimethylamino)-N-[7-hydroxyamino)-7-oxoheptyl]benzamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0040029 | biological_process | epigenetic regulation of gene expression |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0004407 | molecular_function | histone deacetylase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0040029 | biological_process | epigenetic regulation of gene expression |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0004407 | molecular_function | histone deacetylase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0040029 | biological_process | epigenetic regulation of gene expression |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | B3N405 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | ASP193 |
| A | ASP195 |
| A | HIS197 |
| A | SER216 |
| A | LEU217 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 403 |
| Chain | Residue |
| A | PHE206 |
| A | ARG209 |
| A | VAL212 |
| A | TYR243 |
| A | HOH545 |
| A | HOH596 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | ASP104 |
| A | ASP106 |
| A | HOH586 |
| A | HOH652 |
| B | HOH549 |
| B | HOH610 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue B3N A 405 |
| Chain | Residue |
| A | ASP19 |
| A | ASP117 |
| A | HIS158 |
| A | HIS159 |
| A | GLY167 |
| A | TYR168 |
| A | ASP195 |
| A | HIS197 |
| A | PHE225 |
| A | ASP284 |
| A | PRO290 |
| A | ILE291 |
| A | GLY321 |
| A | TYR323 |
| A | ZN401 |
| A | HOH503 |
| A | HOH534 |
| A | HOH572 |
| B | PHE91 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | B3N406 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | ASP193 |
| B | ASP195 |
| B | HIS197 |
| B | SER216 |
| B | LEU217 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue K B 403 |
| Chain | Residue |
| B | PHE206 |
| B | ARG209 |
| B | VAL212 |
| B | TYR243 |
| B | HOH512 |
| B | HOH558 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| A | HOH579 |
| A | HOH646 |
| B | ASP104 |
| B | ASP106 |
| B | HOH625 |
| B | HOH629 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 405 |
| Chain | Residue |
| B | GLU288 |
| B | HOH517 |
| B | HOH534 |
| B | HOH582 |
| B | HOH611 |
| B | HOH664 |
| site_id | AD2 |
| Number of Residues | 18 |
| Details | binding site for residue B3N B 406 |
| Chain | Residue |
| A | PHE91 |
| B | ASP19 |
| B | ASP117 |
| B | HIS158 |
| B | HIS159 |
| B | GLY167 |
| B | TYR168 |
| B | ASP195 |
| B | HIS197 |
| B | PHE225 |
| B | ASP284 |
| B | ILE291 |
| B | GLY321 |
| B | TYR323 |
| B | ZN401 |
| B | HOH505 |
| B | HOH524 |
| B | HOH525 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 401 |
| Chain | Residue |
| C | ASP195 |
| C | HIS197 |
| C | ASP284 |
| C | B3N405 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue K C 402 |
| Chain | Residue |
| C | ASP193 |
| C | ASP195 |
| C | HIS197 |
| C | SER216 |
| C | LEU217 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue K C 403 |
| Chain | Residue |
| C | HOH554 |
| C | PHE206 |
| C | ARG209 |
| C | VAL212 |
| C | TYR243 |
| C | HOH546 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 404 |
| Chain | Residue |
| C | ASP104 |
| C | ASP106 |
| C | HOH615 |
| C | HOH634 |
| D | HOH542 |
| D | HOH616 |
| site_id | AD7 |
| Number of Residues | 18 |
| Details | binding site for residue B3N C 405 |
| Chain | Residue |
| C | ASP19 |
| C | ASP117 |
| C | HIS158 |
| C | HIS159 |
| C | GLY167 |
| C | TYR168 |
| C | ASP195 |
| C | HIS197 |
| C | PHE225 |
| C | ASP284 |
| C | ILE291 |
| C | GLY321 |
| C | TYR323 |
| C | ZN401 |
| C | HOH505 |
| C | HOH532 |
| C | HOH538 |
| D | PHE91 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 401 |
| Chain | Residue |
| D | ASP195 |
| D | HIS197 |
| D | ASP284 |
| D | B3N405 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue K D 402 |
| Chain | Residue |
| D | ASP193 |
| D | ASP195 |
| D | HIS197 |
| D | SER216 |
| D | LEU217 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue K D 403 |
| Chain | Residue |
| D | PHE206 |
| D | ARG209 |
| D | VAL212 |
| D | TYR243 |
| D | HOH526 |
| D | HOH603 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 404 |
| Chain | Residue |
| C | HOH524 |
| C | HOH630 |
| D | ASP104 |
| D | ASP106 |
| D | HOH606 |
| D | HOH624 |
| site_id | AE3 |
| Number of Residues | 18 |
| Details | binding site for residue B3N D 405 |
| Chain | Residue |
| C | PHE91 |
| D | ASP19 |
| D | ASP117 |
| D | HIS158 |
| D | HIS159 |
| D | GLY167 |
| D | TYR168 |
| D | ASP195 |
| D | HIS197 |
| D | PHE225 |
| D | ASP284 |
| D | ILE291 |
| D | GLY321 |
| D | TYR323 |
| D | ZN401 |
| D | HOH502 |
| D | HOH512 |
| D | HOH599 |
