2VCG
Crystal structure of a HDAC-like protein HDAH from Bordetella sp. with the bound inhibitor ST-17
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0016787 | molecular_function | hydrolase activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0016787 | molecular_function | hydrolase activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| C | 0006338 | biological_process | chromatin remodeling |
| C | 0016787 | molecular_function | hydrolase activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| D | 0006338 | biological_process | chromatin remodeling |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D1376 |
| Chain | Residue |
| C | THR222 |
| C | GOL1376 |
| D | MET1 |
| D | HIS64 |
| D | VAL337 |
| D | HOH2120 |
| D | HOH2441 |
| D | HOH2442 |
| D | HOH2443 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C1376 |
| Chain | Residue |
| C | TYR220 |
| C | THR222 |
| D | MET1 |
| D | GOL1376 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A1375 |
| Chain | Residue |
| A | ASP186 |
| A | HIS188 |
| A | ASP274 |
| A | S171378 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B1376 |
| Chain | Residue |
| B | ASP186 |
| B | HIS188 |
| B | ASP274 |
| B | S171379 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C1377 |
| Chain | Residue |
| C | ASP186 |
| C | HIS188 |
| C | ASP274 |
| C | S171380 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1377 |
| Chain | Residue |
| D | ASP186 |
| D | HIS188 |
| D | ASP274 |
| D | S171381 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D1378 |
| Chain | Residue |
| D | HIS4 |
| D | HIS6 |
| D | HIS64 |
| D | CL1382 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A1376 |
| Chain | Residue |
| A | ASP184 |
| A | ASP186 |
| A | HIS188 |
| A | SER207 |
| A | LEU208 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B1377 |
| Chain | Residue |
| B | ASP184 |
| B | ASP186 |
| B | HIS188 |
| B | SER207 |
| B | LEU208 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C1378 |
| Chain | Residue |
| C | ASP184 |
| C | ASP186 |
| C | HIS188 |
| C | SER207 |
| C | LEU208 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D1379 |
| Chain | Residue |
| D | ASP184 |
| D | ASP186 |
| D | HIS188 |
| D | SER207 |
| D | LEU208 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A1377 |
| Chain | Residue |
| A | TRP197 |
| A | ASP200 |
| A | VAL203 |
| A | TYR232 |
| A | HOH2242 |
| A | HOH2269 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B1378 |
| Chain | Residue |
| B | TRP197 |
| B | ASP200 |
| B | VAL203 |
| B | TYR232 |
| B | HOH2308 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K C1379 |
| Chain | Residue |
| C | TRP197 |
| C | ASP200 |
| C | VAL203 |
| C | TYR232 |
| C | HOH2281 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D1380 |
| Chain | Residue |
| D | TRP197 |
| D | ASP200 |
| D | VAL203 |
| D | TYR232 |
| D | HOH2279 |
| D | HOH2304 |
| site_id | BC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE S17 D1381 |
| Chain | Residue |
| A | TYR344 |
| A | GLU346 |
| A | PHE347 |
| D | LEU27 |
| D | ALA28 |
| D | ILE106 |
| D | HIS148 |
| D | HIS149 |
| D | PHE158 |
| D | ASP186 |
| D | HIS188 |
| D | ASP274 |
| D | TYR318 |
| D | ZN1377 |
| D | HOH2246 |
| D | HOH2444 |
| site_id | BC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S17 C1380 |
| Chain | Residue |
| C | HIS149 |
| C | PHE158 |
| C | ASP186 |
| C | HIS188 |
| C | ASP274 |
| C | TYR318 |
| C | ZN1377 |
| C | HOH2065 |
| C | HOH2224 |
| B | TYR344 |
| B | GLU346 |
| B | PHE347 |
| B | HOH2401 |
| C | LEU27 |
| C | ALA28 |
| C | ILE106 |
| C | HIS148 |
| site_id | BC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S17 A1378 |
| Chain | Residue |
| A | LEU27 |
| A | ILE106 |
| A | HIS148 |
| A | HIS149 |
| A | PHE158 |
| A | ASP186 |
| A | HIS188 |
| A | PHE214 |
| A | ASP274 |
| A | TYR318 |
| A | ZN1375 |
| A | HOH2393 |
| D | PRO343 |
| D | GLU346 |
| D | PHE347 |
| D | HOH2399 |
| D | HOH2401 |
| site_id | CC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE S17 B1379 |
| Chain | Residue |
| B | LEU27 |
| B | ASP104 |
| B | ILE106 |
| B | HIS148 |
| B | HIS149 |
| B | PHE158 |
| B | ASP186 |
| B | HIS188 |
| B | PHE214 |
| B | ASP274 |
| B | TYR318 |
| B | ZN1376 |
| B | HOH2448 |
| C | PRO343 |
| C | TYR344 |
| C | PHE347 |
| C | HOH2193 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL D1382 |
| Chain | Residue |
| D | HIS4 |
| D | HIS5 |
| D | HIS6 |
| D | HIS64 |
| D | VAL337 |
| D | ZN1378 |
| D | HOH2441 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:Q48935 |
| Chain | Residue | Details |
| A | ALA150 | |
| B | ALA150 | |
| C | ALA150 | |
| D | ALA150 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:27756124, ECO:0007744|PDB:5G1C |
| Chain | Residue | Details |
| A | VAL187 | |
| D | VAL187 | |
| D | HIS189 | |
| D | ALA275 | |
| A | HIS189 | |
| A | ALA275 | |
| B | VAL187 | |
| B | HIS189 | |
| B | ALA275 | |
| C | VAL187 | |
| C | HIS189 | |
| C | ALA275 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Polarizes the scissile carbonyl of the substrate => ECO:0000250|UniProtKB:Q48935 |
| Chain | Residue | Details |
| A | SER319 | |
| B | SER319 | |
| C | SER319 | |
| D | SER319 |
