4ZUR
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 | 6 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | 7XA404 |
| A | HOH512 |
| A | HOH524 |
| 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 | HOH618 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue 7XA A 404 |
| Chain | Residue |
| A | HIS158 |
| A | HIS159 |
| A | GLY167 |
| A | TYR168 |
| A | ASP195 |
| A | HIS197 |
| A | ASP284 |
| A | TYR323 |
| A | ZN401 |
| A | HOH512 |
| A | HOH524 |
| A | HOH604 |
| A | HOH766 |
| A | HOH812 |
| B | GLU106 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | LYS15 |
| A | LYS84 |
| A | GLY85 |
| A | HOH546 |
| A | HOH628 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | 7XA404 |
| B | HOH526 |
| B | HOH527 |
| site_id | AC7 |
| 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 | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NH4 B 403 |
| Chain | Residue |
| B | PHE206 |
| B | ARG209 |
| B | VAL212 |
| B | THR243 |
| B | HOH607 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue 7XA B 404 |
| Chain | Residue |
| A | THR90 |
| B | HIS158 |
| B | HIS159 |
| B | GLY167 |
| B | ASP195 |
| B | HIS197 |
| B | ASP284 |
| B | TYR323 |
| B | ZN401 |
| B | HOH526 |
| B | HOH527 |
| B | HOH533 |
| B | HOH575 |
| B | HOH790 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 405 |
| Chain | Residue |
| B | LYS15 |
| B | TRP75 |
| B | LYS84 |
| B | GLY85 |
| B | HOH520 |
| B | HOH532 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 406 |
| Chain | Residue |
| A | HOH536 |
| A | HOH556 |
| B | ARG96 |
| B | THR97 |
| B | HOH501 |
| B | HOH807 |
| B | HOH808 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:21268586, ECO:0000305|PubMed:26200446 |
| Chain | Residue | Details |
| A | HIS159 | |
| B | HIS159 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0007744|PDB:3Q9E |
| Chain | Residue | Details |
| A | TYR19 | |
| A | GLU117 | |
| A | TYR323 | |
| B | TYR19 | |
| B | GLU117 | |
| B | TYR323 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0007744|PDB:3Q9C |
| Chain | Residue | Details |
| A | GLU106 | |
| B | GLU106 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21268586, ECO:0000269|PubMed:26200446, ECO:0007744|PDB:3Q9B, ECO:0007744|PDB:3Q9E |
| Chain | Residue | Details |
| A | ASP195 | |
| A | HIS197 | |
| A | ASP284 | |
| B | ASP195 | |
| B | HIS197 | |
| B | ASP284 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Polarizes the scissile carbonyl of the substrate => ECO:0000305|PubMed:21268586 |
| Chain | Residue | Details |
| A | TYR323 | |
| B | TYR323 |
