Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016835 | molecular_function | carbon-oxygen lyase activity |
| A | 0017001 | biological_process | antibiotic catabolic process |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016835 | molecular_function | carbon-oxygen lyase activity |
| B | 0017001 | biological_process | antibiotic catabolic process |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016835 | molecular_function | carbon-oxygen lyase activity |
| C | 0017001 | biological_process | antibiotic catabolic process |
| C | 0046677 | biological_process | response to antibiotic |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016835 | molecular_function | carbon-oxygen lyase activity |
| D | 0017001 | biological_process | antibiotic catabolic process |
| D | 0046677 | biological_process | response to antibiotic |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 300 |
| Chain | Residue |
| A | GLY107 |
| A | PRO108 |
| A | ASN109 |
| A | GLY110 |
| A | ASP111 |
| A | TRP113 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 300 |
| Chain | Residue |
| B | GLY110 |
| B | ASP111 |
| B | TRP113 |
| B | GLY107 |
| B | PRO108 |
| B | ASN109 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL C 300 |
| Chain | Residue |
| C | GLY107 |
| C | PRO108 |
| C | ASN109 |
| C | GLY110 |
| C | ASP111 |
| C | TRP113 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 300 |
| Chain | Residue |
| D | PRO108 |
| D | ASN109 |
| D | ASP111 |
| D | TRP113 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CL D 301 |
| Chain | Residue |
| D | LEU94 |
| D | PRO95 |
| D | ASN96 |
| D | SER99 |
| D | GLU116 |
| D | ARG121 |
| D | GLU133 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17563376","evidenceCode":"ECO:0000269"}]} |
