6GX3
Crystal structure of Schistosoma mansoni HDAC8 complexed with an hydroxamate 1
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 | 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 | 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 | 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 | 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 | FF2504 |
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 | HOH633 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue FF2 A 504 |
Chain | Residue |
A | ASP100 |
A | HIS141 |
A | HIS142 |
A | GLY150 |
A | PHE151 |
A | ASP186 |
A | HIS188 |
A | PHE216 |
A | ASP285 |
A | HIS292 |
A | GLY339 |
A | TYR341 |
A | ZN501 |
B | ASP50 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue FF2 A 505 |
Chain | Residue |
A | GLU131 |
A | LEU327 |
A | LYS330 |
A | VAL331 |
A | PRO332 |
A | VAL361 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | TYR110 |
A | SER111 |
A | ALA114 |
A | TRP140 |
A | PHE151 |
A | CYS152 |
A | TYR153 |
A | LEU154 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | HIS189 |
A | GLU194 |
A | THR219 |
A | GLY220 |
A | THR221 |
A | ASN223 |
A | PHE233 |
A | LEU234 |
A | ASN246 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | ASP186 |
B | HIS188 |
B | ASP285 |
B | FF2504 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue K B 502 |
Chain | Residue |
B | PHE197 |
B | SER200 |
B | VAL203 |
B | SER243 |
B | HOH670 |
site_id | AD1 |
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 | AD2 |
Number of Residues | 12 |
Details | binding site for residue FF2 B 504 |
Chain | Residue |
A | ASP50 |
B | ASP100 |
B | HIS141 |
B | HIS142 |
B | PHE151 |
B | ASP186 |
B | HIS188 |
B | PHE216 |
B | ASP285 |
B | GLY339 |
B | TYR341 |
B | ZN501 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue FF2 B 505 |
Chain | Residue |
B | GLU131 |
B | LEU327 |
B | LYS330 |
B | VAL331 |
B | VAL361 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | LEU234 |
B | ASN235 |
B | GLY236 |
B | ARG241 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue GOL B 507 |
Chain | Residue |
B | HIS189 |
B | GLU194 |
B | GLY220 |
B | THR221 |
B | PHE233 |
B | LEU234 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue DMF B 508 |
Chain | Residue |
B | TYR301 |
B | ARG352 |
B | ALA355 |
B | LEU356 |
B | GLU359 |
B | MET366 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue ZN C 501 |
Chain | Residue |
C | HIS188 |
C | ASP285 |
C | FF2504 |
C | ASP186 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue K C 502 |
Chain | Residue |
C | PHE197 |
C | SER200 |
C | VAL203 |
C | SER243 |
C | HOH680 |
site_id | AD9 |
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 | AE1 |
Number of Residues | 12 |
Details | binding site for residue FF2 C 504 |
Chain | Residue |
C | HIS141 |
C | HIS142 |
C | GLY150 |
C | PHE151 |
C | ASP186 |
C | HIS188 |
C | PHE216 |
C | ASP285 |
C | HIS292 |
C | GLY339 |
C | TYR341 |
C | ZN501 |
site_id | AE2 |
Number of Residues | 6 |
Details | binding site for residue FF2 C 505 |
Chain | Residue |
C | GLU131 |
C | VAL132 |
C | LEU327 |
C | LYS330 |
C | VAL331 |
C | VAL361 |
site_id | AE3 |
Number of Residues | 7 |
Details | binding site for residue GOL C 506 |
Chain | Residue |
C | HIS189 |
C | GLU194 |
C | THR219 |
C | GLY220 |
C | THR221 |
C | PHE233 |
C | LEU234 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue GOL C 507 |
Chain | Residue |
C | GLN10 |
C | TYR11 |
C | LEU14 |
C | GLN116 |
C | HOH633 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue DMF C 508 |
Chain | Residue |
C | TYR7 |
C | ARG12 |
C | ASP30 |
C | ILE38 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue ZN D 501 |
Chain | Residue |
D | ASP186 |
D | HIS188 |
D | ASP285 |
D | FF2504 |
site_id | AE7 |
Number of Residues | 5 |
Details | binding site for residue K D 502 |
Chain | Residue |
D | PHE197 |
D | SER200 |
D | VAL203 |
D | SER243 |
D | HOH659 |
site_id | AE8 |
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 | AE9 |
Number of Residues | 14 |
Details | binding site for residue FF2 D 504 |
Chain | Residue |
C | ASP50 |
D | ASP100 |
D | HIS141 |
D | HIS142 |
D | GLY150 |
D | PHE151 |
D | ASP186 |
D | HIS188 |
D | PHE216 |
D | ASP285 |
D | HIS292 |
D | GLY339 |
D | TYR341 |
D | ZN501 |
site_id | AF1 |
Number of Residues | 4 |
Details | binding site for residue FF2 D 505 |
Chain | Residue |
D | GLU131 |
D | LYS330 |
D | VAL331 |
D | PRO332 |