6FU1
Crystal structure of Schistosoma mansoni HDAC8 complexed with a n-alkyl hydroxamate
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 | E7Q504 |
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 | HOH694 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue E7Q A 504 |
Chain | Residue |
A | ASP100 |
A | GLY139 |
A | TRP140 |
A | HIS141 |
A | HIS142 |
A | GLY150 |
A | PHE151 |
A | CYS152 |
A | ASP186 |
A | HIS188 |
A | PHE216 |
A | ASP285 |
A | HIS292 |
A | GLY338 |
A | GLY339 |
A | TYR341 |
A | ZN501 |
B | ASP50 |
B | HOH736 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | HIS189 |
A | GLU194 |
A | THR219 |
A | GLY220 |
A | THR221 |
A | ASN223 |
A | PHE233 |
A | LEU234 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue E7Q A 506 |
Chain | Residue |
A | GLY238 |
A | ARG239 |
C | PHE300 |
C | PRO302 |
C | CYS314 |
C | SER315 |
C | ASP388 |
C | PRO393 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | ASP186 |
B | HIS188 |
B | ASP285 |
B | E7Q504 |
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 | HOH701 |
site_id | AD1 |
Number of Residues | 13 |
Details | binding site for residue E7Q B 504 |
Chain | Residue |
B | PHE21 |
B | TRP140 |
B | HIS141 |
B | HIS142 |
B | GLY150 |
B | PHE151 |
B | CYS152 |
B | ASP186 |
B | HIS188 |
B | ASP285 |
B | GLY339 |
B | TYR341 |
B | ZN501 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue E7Q B 505 |
Chain | Residue |
B | PHE300 |
B | PRO302 |
B | CYS314 |
B | SER315 |
B | ASP388 |
B | PRO393 |
D | GLY238 |
D | ARG239 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | HIS189 |
B | GLU194 |
B | GLY220 |
B | THR221 |
B | PHE233 |
B | LEU234 |
B | ASN246 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue ZN C 501 |
Chain | Residue |
C | ASP186 |
C | HIS188 |
C | ASP285 |
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 | 4 |
Details | binding site for residue K C 503 |
Chain | Residue |
C | PHE197 |
C | SER200 |
C | VAL203 |
C | SER243 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue GOL C 504 |
Chain | Residue |
C | HIS189 |
C | GLU194 |
C | GLY220 |
C | THR221 |
C | PHE233 |
C | LEU234 |
site_id | AD8 |
Number of Residues | 3 |
Details | binding site for residue ZN D 501 |
Chain | Residue |
D | ASP186 |
D | HIS188 |
D | ASP285 |
site_id | AD9 |
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 | AE1 |
Number of Residues | 5 |
Details | binding site for residue K D 503 |
Chain | Residue |
D | PHE197 |
D | SER200 |
D | VAL203 |
D | SER243 |
D | HOH699 |