1T64
Crystal Structure of human HDAC8 complexed with Trichostatin A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000118 | cellular_component | histone deacetylase complex |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000228 | cellular_component | nuclear chromosome |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005694 | cellular_component | chromosome |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006325 | biological_process | chromatin organization |
| A | 0007064 | biological_process | mitotic sister chromatid cohesion |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0030544 | molecular_function | Hsp70 protein binding |
| A | 0031397 | biological_process | negative regulation of protein ubiquitination |
| A | 0031647 | biological_process | regulation of protein stability |
| A | 0032204 | biological_process | regulation of telomere maintenance |
| A | 0033558 | molecular_function | protein lysine deacetylase activity |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051879 | molecular_function | Hsp90 protein binding |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 0160008 | molecular_function | protein decrotonylase activity |
| A | 0160009 | molecular_function | histone decrotonylase activity |
| B | 0000118 | cellular_component | histone deacetylase complex |
| B | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| B | 0000228 | cellular_component | nuclear chromosome |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005694 | cellular_component | chromosome |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006325 | biological_process | chromatin organization |
| B | 0007064 | biological_process | mitotic sister chromatid cohesion |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0030544 | molecular_function | Hsp70 protein binding |
| B | 0031397 | biological_process | negative regulation of protein ubiquitination |
| B | 0031647 | biological_process | regulation of protein stability |
| B | 0032204 | biological_process | regulation of telomere maintenance |
| B | 0033558 | molecular_function | protein lysine deacetylase activity |
| B | 0040029 | biological_process | epigenetic regulation of gene expression |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051879 | molecular_function | Hsp90 protein binding |
| B | 0140297 | molecular_function | DNA-binding transcription factor binding |
| B | 0160008 | molecular_function | protein decrotonylase activity |
| B | 0160009 | molecular_function | histone decrotonylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 388 |
| Chain | Residue |
| A | ASP178 |
| A | HIS180 |
| A | ASP267 |
| A | TSN386 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CA A 389 |
| Chain | Residue |
| A | HOH739 |
| A | HOH741 |
| A | HOH1040 |
| A | HOH734 |
| A | HOH735 |
| A | HOH736 |
| A | HOH737 |
| A | HOH738 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 390 |
| Chain | Residue |
| A | ALA68 |
| A | HOH842 |
| A | HOH843 |
| A | HOH844 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 391 |
| Chain | Residue |
| A | PHE189 |
| A | THR192 |
| A | VAL195 |
| A | TYR225 |
| A | HOH426 |
| A | HOH560 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 392 |
| Chain | Residue |
| A | ASP176 |
| A | ASP178 |
| A | HIS180 |
| A | SER199 |
| A | LEU200 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1388 |
| Chain | Residue |
| B | ASP178 |
| B | HIS180 |
| B | ASP267 |
| B | TSN1386 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CA B 1389 |
| Chain | Residue |
| B | HOH725 |
| B | HOH726 |
| B | HOH727 |
| B | HOH728 |
| B | HOH729 |
| B | HOH730 |
| B | HOH731 |
| B | HOH732 |
| B | HOH1066 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 1390 |
| Chain | Residue |
| B | ALA68 |
| B | HOH676 |
| B | HOH771 |
| B | HOH783 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1391 |
| Chain | Residue |
| B | ASP176 |
| B | ASP178 |
| B | HIS180 |
| B | SER199 |
| B | LEU200 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 1392 |
| Chain | Residue |
| B | PHE189 |
| B | THR192 |
| B | VAL195 |
| B | TYR225 |
| B | HOH439 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TSN A 386 |
| Chain | Residue |
| A | TYR100 |
| A | HIS142 |
| A | HIS143 |
| A | GLY151 |
| A | PHE152 |
| A | ASP178 |
| A | HIS180 |
| A | ASP267 |
| A | MET274 |
| A | TYR306 |
| A | TSN387 |
| A | ZN388 |
| A | HOH657 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TSN A 387 |
| Chain | Residue |
| A | ILE34 |
| A | PRO35 |
| A | TYR111 |
| A | TRP141 |
| A | PRO273 |
| A | TYR306 |
| A | TSN386 |
| A | HOH657 |
| A | HOH661 |
| A | HOH992 |
| site_id | BC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TSN B 1386 |
| Chain | Residue |
| B | TYR100 |
| B | HIS142 |
| B | HIS143 |
| B | GLY151 |
| B | PHE152 |
| B | ASP178 |
| B | HIS180 |
| B | ASP267 |
| B | TYR306 |
| B | TSN1387 |
| B | ZN1388 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TSN B 1387 |
| Chain | Residue |
| B | ILE34 |
| B | PRO35 |
| B | TYR111 |
| B | TRP141 |
| B | PHE152 |
| B | PRO273 |
| B | TYR306 |
| B | HOH541 |
| B | HOH581 |
| B | TSN1386 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282 |
| Chain | Residue | Details |
| A | HIS143 | |
| B | HIS143 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19053282 |
| Chain | Residue | Details |
| A | ASP101 | |
| A | GLY151 | |
| A | TYR306 | |
| B | ASP101 | |
| B | GLY151 | |
| B | TYR306 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17721440 |
| Chain | Residue | Details |
| B | HIS180 | |
| B | ASP267 | |
| A | ASP178 | |
| A | HIS180 | |
| A | ASP267 | |
| B | ASP178 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608 |
| Chain | Residue | Details |
| A | SER39 | |
| B | SER39 |
