1R00
Crystal structure of aclacinomycin-10-hydroxylase (RdmB) in complex with S-adenosyl-L-homocysteine (SAH)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008171 | molecular_function | O-methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0032259 | biological_process | methylation |
| A | 0046983 | molecular_function | protein dimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACT A 421 |
| Chain | Residue |
| A | TYR171 |
| A | ASP188 |
| A | GLY191 |
| A | GLY194 |
| A | GLY195 |
| A | MET196 |
| A | LEU197 |
| A | SER255 |
| A | SAH635 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SAH A 635 |
| Chain | Residue |
| A | TRP146 |
| A | TYR171 |
| A | GLY190 |
| A | GLY191 |
| A | GLY192 |
| A | GLU213 |
| A | LEU214 |
| A | PRO217 |
| A | GLY239 |
| A | ASP240 |
| A | PHE241 |
| A | PHE242 |
| A | SER255 |
| A | ASN260 |
| A | TRP261 |
| A | ACT421 |
| A | HOH647 |
| A | HOH712 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14607118","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R00","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14607118","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15548527","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1QZZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R00","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XDS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for 4-O-methylation activity","evidences":[{"source":"PubMed","id":"39308748","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for 10-decarboxylative hydroxylation activity","evidences":[{"source":"PubMed","id":"39308748","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1kyw |
| Chain | Residue | Details |
| A | LEU259 |
