4ZUO
Crystal structure of acetylpolyamine amidohydrolase from Mycoplana ramosa in complex with a hydroxamate inhibitor
Replaces: 4K6QFunctional 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 | 6 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | XS6404 |
| A | HOH511 |
| A | HOH557 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | SER216 |
| A | LEU217 |
| A | ASP193 |
| A | ASP195 |
| A | HIS197 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NH4 A 403 |
| Chain | Residue |
| A | PHE206 |
| A | ARG209 |
| A | VAL212 |
| A | THR243 |
| A | HOH606 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue XS6 A 404 |
| Chain | Residue |
| A | TYR19 |
| A | HIS158 |
| A | HIS159 |
| A | TYR168 |
| A | ASP195 |
| A | HIS197 |
| A | PHE225 |
| A | ASP284 |
| A | TYR323 |
| A | ZN401 |
| A | HOH511 |
| A | HOH557 |
| A | HOH645 |
| A | HOH756 |
| A | HOH800 |
| B | TYR83 |
| B | HOH843 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | ARG96 |
| A | HOH502 |
| B | HOH550 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | LYS15 |
| A | TRP75 |
| A | LYS84 |
| A | GLY85 |
| A | HOH521 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | XS6404 |
| B | HOH539 |
| B | HOH541 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | ASP193 |
| B | ASP195 |
| B | HIS197 |
| B | SER216 |
| B | LEU217 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue NH4 B 403 |
| Chain | Residue |
| B | PHE206 |
| B | ARG209 |
| B | VAL212 |
| B | THR243 |
| B | THR244 |
| B | HOH612 |
| B | HOH684 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue XS6 B 404 |
| Chain | Residue |
| A | TYR83 |
| B | HIS158 |
| B | HIS159 |
| B | GLY167 |
| B | TYR168 |
| B | ASP195 |
| B | HIS197 |
| B | PHE225 |
| B | ASP284 |
| B | TYR323 |
| B | ZN401 |
| B | HOH539 |
| B | HOH541 |
| B | HOH574 |
| B | HOH785 |
| B | HOH795 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| A | HOH553 |
| B | ARG96 |
| B | HOH504 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| B | LYS15 |
| B | LYS84 |
| B | GLY85 |
| B | HOH532 |
| B | HOH647 |
| B | HOH687 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 407 |
| Chain | Residue |
| B | ALA245 |
| B | ASN246 |
| B | TYR247 |
| B | ARG268 |
| B | HOH503 |
| B | HOH507 |
| B | HOH508 |
| B | HOH650 |
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 |
