Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | ASN109 |
A | ASP125 |
A | ASP129 |
A | HOH442 |
A | HOH459 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CA A 302 |
Chain | Residue |
A | GLU127 |
A | ASP129 |
A | ASP143 |
A | HOH442 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue GOL A 303 |
Chain | Residue |
A | ARG20 |
A | ASP22 |
A | ILE30 |
A | TYR32 |
A | HIS66 |
A | TRP68 |
A | TRP93 |
A | ASP125 |
A | HOH410 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue GOL A 304 |
Chain | Residue |
A | SER136 |
A | ARG137 |
A | PHE139 |
A | ILE175 |
A | HOH414 |
A | HOH458 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue GOL A 305 |
Chain | Residue |
A | GLU105 |
A | ARG140 |
A | HOH413 |
A | HOH416 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS142 | |
Chain | Residue | Details |
A | TRP68 | |
A | ARG74 | |
A | GLN76 | |
A | SER77 | |
A | LYS142 | |
Chain | Residue | Details |
A | ASN109 | |
A | ASP125 | |
A | GLU127 | |
A | ASP129 | |
A | ASP143 | |