5THS
Crystal Structure of G302A HDAC8 in complex with M344
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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0031507 | biological_process | heterochromatin formation |
| 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 | 0046872 | molecular_function | metal ion binding |
| A | 0051879 | molecular_function | Hsp90 protein binding |
| A | 0140297 | molecular_function | DNA-binding transcription factor binding |
| A | 0141221 | molecular_function | histone deacetylase activity, hydrolytic mechanism |
| 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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0031507 | biological_process | heterochromatin formation |
| 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 | 0046872 | molecular_function | metal ion binding |
| B | 0051879 | molecular_function | Hsp90 protein binding |
| B | 0140297 | molecular_function | DNA-binding transcription factor binding |
| B | 0141221 | molecular_function | histone deacetylase activity, hydrolytic mechanism |
| 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 401 |
| Chain | Residue |
| A | ASP178 |
| A | HIS180 |
| A | ASP267 |
| A | B3N404 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | ASP176 |
| A | ASP178 |
| A | HIS180 |
| A | SER199 |
| A | LEU200 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue K A 403 |
| Chain | Residue |
| A | PHE189 |
| A | THR192 |
| A | VAL195 |
| A | TYR225 |
| A | HOH515 |
| A | HOH600 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue B3N A 404 |
| Chain | Residue |
| A | ASP101 |
| A | HIS142 |
| A | HIS143 |
| A | ASP178 |
| A | HIS180 |
| A | ASP267 |
| A | TYR306 |
| A | ZN401 |
| A | EDO411 |
| A | HOH595 |
| A | HOH597 |
| B | PHE152 |
| B | PRO273 |
| B | TYR306 |
| B | B3N404 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ALA270 |
| A | ASN310 |
| A | ILE348 |
| A | THR349 |
| A | HOH551 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | PRO281 |
| A | VAL282 |
| A | TYR317 |
| A | LEU346 |
| A | GLU347 |
| A | ILE348 |
| A | HOH564 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | VAL133 |
| A | LEU292 |
| A | GLN295 |
| A | LEU296 |
| A | THR298 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | ASP237 |
| A | VAL282 |
| A | LYS286 |
| A | HOH501 |
| A | HOH526 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | LYS239 |
| A | ASP355 |
| A | HOH541 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | TYR111 |
| A | ILE115 |
| A | TRP141 |
| A | CYS153 |
| A | TYR154 |
| A | LEU155 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | GLY140 |
| A | TRP141 |
| A | GLY303 |
| A | TYR306 |
| A | B3N404 |
| A | HOH575 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP178 |
| B | HIS180 |
| B | ASP267 |
| B | B3N404 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | ASP176 |
| B | ASP178 |
| B | HIS180 |
| B | SER199 |
| B | LEU200 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue K B 403 |
| Chain | Residue |
| B | PHE189 |
| B | THR192 |
| B | VAL195 |
| B | TYR225 |
| B | HOH520 |
| B | HOH590 |
| site_id | AD6 |
| Number of Residues | 17 |
| Details | binding site for residue B3N B 404 |
| Chain | Residue |
| A | PHE152 |
| A | PRO273 |
| A | MET274 |
| A | TYR306 |
| A | B3N404 |
| B | HIS142 |
| B | HIS143 |
| B | PHE152 |
| B | ASP178 |
| B | HIS180 |
| B | ASP267 |
| B | GLY304 |
| B | TYR306 |
| B | ZN401 |
| B | EDO405 |
| B | EDO408 |
| B | HOH562 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | GLY140 |
| B | TRP141 |
| B | HIS142 |
| B | GLY303 |
| B | GLY304 |
| B | TYR306 |
| B | B3N404 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | PRO281 |
| B | TYR317 |
| B | LEU346 |
| B | GLU347 |
| B | ILE348 |
| B | HOH506 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | ILE34 |
| B | ARG37 |
| B | ALA38 |
| B | VAL41 |
| B | TRP137 |
| B | SER138 |
| B | TRP315 |
| site_id | AE1 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | SER150 |
| B | GLY151 |
| B | PHE208 |
| B | B3N404 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 409 |
| Chain | Residue |
| B | LYS289 |
| B | GLY324 |
| B | LYS325 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 410 |
| Chain | Residue |
| B | TRP141 |
| B | PHE152 |
| B | TYR154 |
| B | LEU155 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 310 |
| Details | Region: {"description":"Histone deacetylase"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19053282","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19053282","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17721440","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15242608","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
