6HSZ
Crystal structure of Schistosoma mansoni HDAC8 complexed with a benzohydroxamate inhibitor 2
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 | GOW504 |
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 | HOH659 |
site_id | AC4 |
Number of Residues | 12 |
Details | binding site for residue GOW A 504 |
Chain | Residue |
A | LYS20 |
A | HIS141 |
A | HIS142 |
A | GLY150 |
A | ASP186 |
A | HIS188 |
A | PHE216 |
A | ASP285 |
A | HIS292 |
A | TYR341 |
A | ZN501 |
B | ASP50 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | HIS188 |
A | HIS189 |
A | HIS210 |
A | ALA211 |
A | SER212 |
A | PHE215 |
A | PHE216 |
A | PRO217 |
A | GLY218 |
A | THR219 |
A | HOH647 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | HIS189 |
A | GLU194 |
A | THR219 |
A | GLY220 |
A | THR221 |
A | PHE233 |
A | LEU234 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | ASP186 |
B | HIS188 |
B | ASP285 |
B | GOW504 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue K B 502 |
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 503 |
Chain | Residue |
B | PHE197 |
B | SER200 |
B | VAL203 |
B | SER243 |
B | HOH666 |
site_id | AD1 |
Number of Residues | 12 |
Details | binding site for residue GOW B 504 |
Chain | Residue |
A | ASP50 |
B | LYS20 |
B | HIS141 |
B | HIS142 |
B | ASP186 |
B | HIS188 |
B | PHE216 |
B | ASP285 |
B | PRO291 |
B | HIS292 |
B | TYR341 |
B | ZN501 |
site_id | AD2 |
Number of Residues | 7 |
Details | binding site for residue GOL B 505 |
Chain | Residue |
B | HIS189 |
B | GLU194 |
B | THR219 |
B | GLY220 |
B | THR221 |
B | PHE233 |
B | LEU234 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | TYR35 |
B | LYS36 |
B | MET366 |
B | THR367 |
D | LYS82 |
D | THR85 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue ZN C 501 |
Chain | Residue |
C | ASP186 |
C | HIS188 |
C | ASP285 |
C | GOW504 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue K C 502 |
Chain | Residue |
C | ASP184 |
C | ASP186 |
C | HIS188 |
C | SER207 |
C | VAL208 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue K C 503 |
Chain | Residue |
C | PHE197 |
C | SER200 |
C | VAL203 |
C | SER243 |
C | HOH675 |
site_id | AD7 |
Number of Residues | 13 |
Details | binding site for residue GOW C 504 |
Chain | Residue |
C | HIS142 |
C | ASP186 |
C | HIS188 |
C | PHE216 |
C | ASP285 |
C | PRO291 |
C | HIS292 |
C | TYR341 |
C | ZN501 |
C | HOH664 |
D | ASP50 |
C | LYS20 |
C | HIS141 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue GOL C 505 |
Chain | Residue |
C | CYS15 |
C | PHE21 |
C | GLY22 |
C | ARG24 |
C | TYR25 |
C | TRP136 |
C | GLY137 |
C | TRP140 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue ZN D 501 |
Chain | Residue |
D | ASP186 |
D | HIS188 |
D | ASP285 |
D | GOW504 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue K D 502 |
Chain | Residue |
D | ASP184 |
D | ASP186 |
D | HIS188 |
D | SER207 |
D | VAL208 |
site_id | AE2 |
Number of Residues | 5 |
Details | binding site for residue K D 503 |
Chain | Residue |
D | PHE197 |
D | SER200 |
D | VAL203 |
D | SER243 |
D | HOH648 |
site_id | AE3 |
Number of Residues | 12 |
Details | binding site for residue GOW D 504 |
Chain | Residue |
C | ASP50 |
D | LYS20 |
D | HIS141 |
D | HIS142 |
D | ASP186 |
D | HIS188 |
D | ASP285 |
D | PRO291 |
D | HIS292 |
D | GLY339 |
D | TYR341 |
D | ZN501 |
site_id | AE4 |
Number of Residues | 7 |
Details | binding site for residue GOL D 505 |
Chain | Residue |
D | HIS189 |
D | GLU194 |
D | GLY220 |
D | THR221 |
D | ASN223 |
D | LEU234 |
D | ASN246 |
site_id | AE5 |
Number of Residues | 9 |
Details | binding site for residue GOL D 506 |
Chain | Residue |
D | CYS15 |
D | PHE21 |
D | ARG24 |
D | TYR25 |
D | TYR110 |
D | TRP136 |
D | GLY137 |
D | TRP140 |
D | HOH655 |