6PHT
Crystal structure of Marinobacter subterrani acetylpolyamine amidohydrolase (msAPAH) complexed with 5-[(3-aminopropyl)amino]pentylboronic acid
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 | 15 |
| Details | binding site for residue OKP A 401 |
| Chain | Residue |
| A | ASP117 |
| A | GLY321 |
| A | TYR323 |
| A | ZN406 |
| A | HOH509 |
| A | HOH527 |
| A | HOH621 |
| A | HIS158 |
| A | HIS159 |
| A | GLY167 |
| A | TYR168 |
| A | ASP195 |
| A | HIS197 |
| A | PHE225 |
| A | ASP284 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | PHE206 |
| A | ARG209 |
| A | VAL212 |
| A | TYR243 |
| A | HOH523 |
| A | HOH533 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K A 403 |
| Chain | Residue |
| A | ASP193 |
| A | ASP195 |
| A | HIS197 |
| A | SER216 |
| A | LEU217 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue MG A 404 |
| Chain | Residue |
| A | LYS83 |
| A | ASP104 |
| A | ASP106 |
| A | HOH544 |
| A | HOH580 |
| C | HOH542 |
| C | HOH585 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 405 |
| Chain | Residue |
| A | GLU288 |
| A | HOH503 |
| A | HOH605 |
| A | HOH629 |
| A | HOH635 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 406 |
| Chain | Residue |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | OKP401 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue OKP B 401 |
| Chain | Residue |
| B | GLU17 |
| B | HIS158 |
| B | HIS159 |
| B | GLY167 |
| B | TYR168 |
| B | ASP195 |
| B | HIS197 |
| B | PHE225 |
| B | ASP284 |
| B | GLY321 |
| B | TYR323 |
| B | ZN405 |
| B | HOH502 |
| B | HOH545 |
| B | HOH607 |
| D | PHE91 |
| D | HOH556 |
| D | HOH633 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | PHE206 |
| B | ARG209 |
| B | VAL212 |
| B | TYR243 |
| B | HOH528 |
| B | HOH557 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue K B 403 |
| Chain | Residue |
| B | ASP193 |
| B | ASP195 |
| B | HIS197 |
| B | SER216 |
| B | LEU217 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 404 |
| Chain | Residue |
| B | ASP104 |
| B | ASP106 |
| B | HOH542 |
| B | HOH553 |
| D | HOH541 |
| D | HOH566 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 405 |
| Chain | Residue |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | OKP401 |
| site_id | AD3 |
| Number of Residues | 18 |
| Details | binding site for residue OKP C 401 |
| Chain | Residue |
| A | PHE91 |
| C | ASP117 |
| C | HIS158 |
| C | HIS159 |
| C | GLY167 |
| C | TYR168 |
| C | ASP195 |
| C | HIS197 |
| C | PHE225 |
| C | ASP284 |
| C | GLY321 |
| C | TYR323 |
| C | ZN405 |
| C | HOH501 |
| C | HOH508 |
| C | HOH524 |
| C | HOH602 |
| C | HOH636 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue K C 402 |
| Chain | Residue |
| C | PHE206 |
| C | ARG209 |
| C | VAL212 |
| C | TYR243 |
| C | HOH522 |
| C | HOH547 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue K C 403 |
| Chain | Residue |
| C | ASP193 |
| C | ASP195 |
| C | HIS197 |
| C | SER216 |
| C | LEU217 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 404 |
| Chain | Residue |
| A | HOH517 |
| A | HOH595 |
| C | ASP104 |
| C | ASP106 |
| C | HOH535 |
| C | HOH616 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 405 |
| Chain | Residue |
| C | ASP195 |
| C | HIS197 |
| C | ASP284 |
| C | OKP401 |
| site_id | AD8 |
| Number of Residues | 19 |
| Details | binding site for residue OKP D 401 |
| Chain | Residue |
| B | PHE91 |
| D | ASP117 |
| D | HIS158 |
| D | HIS159 |
| D | GLY167 |
| D | TYR168 |
| D | ASP195 |
| D | HIS197 |
| D | PHE225 |
| D | ASP284 |
| D | GLY321 |
| D | TYR323 |
| D | ZN405 |
| D | HOH501 |
| D | HOH502 |
| D | HOH515 |
| D | HOH544 |
| D | HOH607 |
| D | HOH627 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue K D 402 |
| Chain | Residue |
| D | PHE206 |
| D | ARG209 |
| D | VAL212 |
| D | TYR243 |
| D | HOH509 |
| D | HOH546 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue K D 403 |
| Chain | Residue |
| D | ASP193 |
| D | ASP195 |
| D | HIS197 |
| D | SER216 |
| D | LEU217 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue MG D 404 |
| Chain | Residue |
| B | HOH522 |
| B | HOH567 |
| D | LYS83 |
| D | ASP104 |
| D | ASP106 |
| D | HOH531 |
| D | HOH580 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 405 |
| Chain | Residue |
| D | ASP195 |
| D | HIS197 |
| D | ASP284 |
| D | OKP401 |
