6CBK
X-ray structure of NeoB from Streptomyces fradiae in complex with PMP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017000 | biological_process | antibiotic biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 1901158 | biological_process | neomycin biosynthetic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0017000 | biological_process | antibiotic biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 1901158 | biological_process | neomycin biosynthetic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0017000 | biological_process | antibiotic biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 1901158 | biological_process | neomycin biosynthetic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0017000 | biological_process | antibiotic biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 1901158 | biological_process | neomycin biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue PMP A 501 |
| Chain | Residue |
| A | SER103 |
| A | LYS231 |
| A | HOH659 |
| A | HOH680 |
| A | HOH752 |
| B | PHE257 |
| B | THR258 |
| A | GLY104 |
| A | THR105 |
| A | TYR129 |
| A | HIS130 |
| A | GLY131 |
| A | SER176 |
| A | ASP204 |
| A | VAL206 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | LEU53 |
| A | ASP57 |
| A | ARG275 |
| A | HOH611 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue PMP B 501 |
| Chain | Residue |
| A | PHE257 |
| A | THR258 |
| B | GLY104 |
| B | THR105 |
| B | TYR129 |
| B | HIS130 |
| B | GLY131 |
| B | SER176 |
| B | ASP204 |
| B | VAL206 |
| B | LYS207 |
| B | LYS231 |
| B | HIS424 |
| B | HOH604 |
| B | HOH632 |
| B | HOH634 |
| B | HOH736 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue PMP C 501 |
| Chain | Residue |
| C | SER103 |
| C | GLY104 |
| C | THR105 |
| C | TYR129 |
| C | HIS130 |
| C | GLY131 |
| C | SER176 |
| C | ASP204 |
| C | VAL206 |
| C | LYS207 |
| C | LYS231 |
| C | HOH606 |
| C | HOH613 |
| C | HOH695 |
| C | HOH722 |
| D | PHE257 |
| D | THR258 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 502 |
| Chain | Residue |
| B | HOH775 |
| C | THR69 |
| D | ALA28 |
| D | SER29 |
| D | HOH793 |
| D | HOH832 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue PMP D 501 |
| Chain | Residue |
| C | PHE257 |
| C | THR258 |
| D | GLY104 |
| D | THR105 |
| D | TYR129 |
| D | HIS130 |
| D | GLY131 |
| D | SER176 |
| D | ASP204 |
| D | VAL206 |
| D | LYS231 |
| D | HIS424 |
| D | HOH623 |
| D | HOH712 |
| D | HOH751 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
