4ZUQ
Crystal structure of acetylpolyamine amidohydrolase from Mycoplana ramosa in complex with a hydroxamate inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004407 | molecular_function | histone deacetylase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0040029 | biological_process | epigenetic regulation of gene expression |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0047609 | molecular_function | acetylputrescine deacetylase activity |
| A | 0047611 | molecular_function | acetylspermidine deacetylase activity |
| B | 0004407 | molecular_function | histone deacetylase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0040029 | biological_process | epigenetic regulation of gene expression |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047609 | molecular_function | acetylputrescine deacetylase activity |
| B | 0047611 | molecular_function | acetylspermidine deacetylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue K A 401 |
| Chain | Residue |
| A | ASP193 |
| A | ASP195 |
| A | HIS197 |
| A | SER216 |
| A | LEU217 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | HOH705 |
| A | PHE206 |
| A | ARG209 |
| A | VAL212 |
| A | THR243 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue 6XA A 403 |
| Chain | Residue |
| A | GLU17 |
| A | GLU117 |
| A | HIS158 |
| A | HIS159 |
| A | GLY167 |
| A | TYR168 |
| A | ASP195 |
| A | HIS197 |
| A | PHE225 |
| A | ASP284 |
| A | TYR323 |
| A | ZN404 |
| A | HOH504 |
| A | HOH572 |
| A | HOH597 |
| A | HOH739 |
| A | HOH769 |
| B | HOH503 |
| B | HOH590 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 404 |
| Chain | Residue |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | 6XA403 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 405 |
| Chain | Residue |
| A | HIS146 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | LYS15 |
| A | LYS84 |
| A | GLY85 |
| A | HOH531 |
| A | HOH533 |
| A | HOH559 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | ARG96 |
| A | HOH535 |
| B | HOH550 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 401 |
| Chain | Residue |
| B | ASP193 |
| B | ASP195 |
| B | HIS197 |
| B | SER216 |
| B | LEU217 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 402 |
| Chain | Residue |
| B | PHE206 |
| B | ARG209 |
| B | VAL212 |
| B | THR243 |
| B | HOH715 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for residue 6XA B 403 |
| Chain | Residue |
| A | HOH884 |
| B | GLU17 |
| B | GLU117 |
| B | HIS158 |
| B | HIS159 |
| B | TYR168 |
| B | ASP195 |
| B | HIS197 |
| B | PHE225 |
| B | ASP284 |
| B | TYR323 |
| B | ZN404 |
| B | HOH528 |
| B | HOH573 |
| B | HOH626 |
| B | HOH739 |
| B | HOH752 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 404 |
| Chain | Residue |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | 6XA403 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue ZN B 405 |
| Chain | Residue |
| B | HIS146 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | LYS15 |
| B | LYS84 |
| B | GLY85 |
| B | HOH506 |
| B | HOH535 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 407 |
| Chain | Residue |
| A | HOH544 |
| B | ARG96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"21268586","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26200446","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21268586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q9E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21268586","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q9C","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21268586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26200446","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q9B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q9E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Polarizes the scissile carbonyl of the substrate","evidences":[{"source":"PubMed","id":"21268586","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
