6HTI
Crystal structure of Schistosoma mansoni HDAC8 complexed with a benzohydroxamate inhibitor 6
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| C | 0004407 | molecular_function | histone deacetylase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006338 | biological_process | chromatin remodeling |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| D | 0004407 | molecular_function | histone deacetylase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006338 | biological_process | chromatin remodeling |
| 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 501 |
| Chain | Residue |
| A | ASP186 |
| A | HIS188 |
| A | ASP285 |
| A | GQW505 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 502 |
| Chain | Residue |
| A | ASP184 |
| A | ASP186 |
| A | HIS188 |
| A | SER207 |
| A | VAL208 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue K A 503 |
| Chain | Residue |
| A | PHE197 |
| A | SER200 |
| A | VAL203 |
| A | SER243 |
| A | HOH672 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | HIS189 |
| A | GLU194 |
| A | THR219 |
| A | GLY220 |
| A | THR221 |
| A | ASN223 |
| A | LEU234 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | binding site for residue GQW A 505 |
| Chain | Residue |
| A | LYS20 |
| A | HIS141 |
| A | HIS142 |
| A | ASP186 |
| A | HIS188 |
| A | PHE216 |
| A | ASP285 |
| A | HIS292 |
| A | GLY339 |
| A | TYR341 |
| A | ZN501 |
| B | ASP50 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue GQW B 501 |
| Chain | Residue |
| A | ASP50 |
| B | LYS20 |
| B | HIS141 |
| B | HIS142 |
| B | GLY150 |
| B | ASP186 |
| B | HIS188 |
| B | PHE216 |
| B | ASP285 |
| B | HIS292 |
| B | TYR341 |
| B | ZN502 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | ASP186 |
| B | HIS188 |
| B | ASP285 |
| B | GQW501 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 503 |
| Chain | Residue |
| B | ASP184 |
| B | ASP186 |
| B | HIS188 |
| B | SER207 |
| B | VAL208 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue K B 504 |
| Chain | Residue |
| B | PHE197 |
| B | SER200 |
| B | VAL203 |
| B | SER243 |
| B | HOH675 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | HIS189 |
| B | GLU194 |
| B | THR219 |
| B | GLY220 |
| B | THR221 |
| B | LEU234 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue GQW C 501 |
| Chain | Residue |
| C | LYS20 |
| C | HIS141 |
| C | HIS142 |
| C | ASP186 |
| C | HIS188 |
| C | PHE216 |
| C | ASP285 |
| C | HIS292 |
| C | TYR341 |
| C | ZN502 |
| D | ASP50 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | ASP186 |
| C | HIS188 |
| C | ASP285 |
| C | GQW501 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue K C 503 |
| Chain | Residue |
| C | ASP184 |
| C | ASP186 |
| C | HIS188 |
| C | SER207 |
| C | VAL208 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue K C 504 |
| Chain | Residue |
| C | PHE197 |
| C | SER200 |
| C | VAL203 |
| C | SER243 |
| C | HOH701 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 505 |
| Chain | Residue |
| C | HIS189 |
| C | GLU194 |
| C | THR219 |
| C | GLY220 |
| C | THR221 |
| C | LEU234 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue GQW D 501 |
| Chain | Residue |
| D | HIS142 |
| D | ASP186 |
| D | HIS188 |
| D | PHE216 |
| D | ASP285 |
| D | HIS292 |
| D | TYR341 |
| D | ZN502 |
| C | ASP50 |
| D | LYS20 |
| D | HIS141 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | ASP186 |
| D | HIS188 |
| D | ASP285 |
| D | GQW501 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue K D 503 |
| Chain | Residue |
| D | ASP184 |
| D | ASP186 |
| D | HIS188 |
| D | SER207 |
| D | VAL208 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue K D 504 |
| Chain | Residue |
| D | PHE197 |
| D | SER200 |
| D | VAL203 |
| D | SER243 |
| D | HOH649 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 505 |
| Chain | Residue |
| D | HIS189 |
| D | GLU194 |
| D | THR219 |
| D | GLY220 |
| D | THR221 |
| D | ASN223 |
| D | LEU234 |
| D | ASN246 |
