5BK7
The structure of MppP E15A mutant soaked with the substrate L-arginine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0008483 | molecular_function | transaminase activity |
| G | 0009058 | biological_process | biosynthetic process |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0008483 | molecular_function | transaminase activity |
| H | 0009058 | biological_process | biosynthetic process |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue EQJ A 400 |
| Chain | Residue |
| A | THR12 |
| A | THR156 |
| A | ASN160 |
| A | ASP188 |
| A | PHE191 |
| A | LYS221 |
| A | LYS229 |
| A | ARG352 |
| A | HOH510 |
| A | HOH522 |
| B | SER248 |
| A | ASP27 |
| B | ASP249 |
| B | ILE250 |
| B | LEU251 |
| A | GLY28 |
| A | HIS29 |
| A | SER89 |
| A | SER90 |
| A | SER91 |
| A | PHE115 |
| A | ASN117 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | binding site for residue EQJ B 401 |
| Chain | Residue |
| A | SER248 |
| A | ASP249 |
| A | ILE250 |
| A | HOH505 |
| B | THR12 |
| B | ASP27 |
| B | GLY28 |
| B | HIS29 |
| B | SER89 |
| B | SER90 |
| B | SER91 |
| B | PHE115 |
| B | ASN117 |
| B | THR156 |
| B | ASN160 |
| B | ASP188 |
| B | PHE191 |
| B | LYS221 |
| B | LYS229 |
| B | ARG352 |
| B | HOH517 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue EQJ C 401 |
| Chain | Residue |
| C | THR12 |
| C | ASP27 |
| C | GLY28 |
| C | HIS29 |
| C | SER89 |
| C | SER90 |
| C | SER91 |
| C | PHE115 |
| C | ASN117 |
| C | THR156 |
| C | ASN160 |
| C | ASP188 |
| C | PHE191 |
| C | LYS221 |
| C | LYS229 |
| C | ARG352 |
| D | SER248 |
| D | ASP249 |
| D | ILE250 |
| D | LEU251 |
| D | HOH506 |
| D | HOH575 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue EQJ D 401 |
| Chain | Residue |
| C | SER248 |
| C | ASP249 |
| C | ILE250 |
| D | THR12 |
| D | ASP27 |
| D | GLY28 |
| D | HIS29 |
| D | SER89 |
| D | SER90 |
| D | SER91 |
| D | PHE115 |
| D | ASN117 |
| D | THR156 |
| D | ASN160 |
| D | ASP188 |
| D | PHE191 |
| D | LYS221 |
| D | LYS229 |
| D | ARG352 |
| D | HOH519 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue EQJ E 401 |
| Chain | Residue |
| E | ARG352 |
| E | HOH515 |
| E | HOH519 |
| F | SER248 |
| F | ASP249 |
| F | ILE250 |
| E | THR12 |
| E | ASP27 |
| E | GLY28 |
| E | SER89 |
| E | SER90 |
| E | SER91 |
| E | PHE115 |
| E | THR156 |
| E | ASN160 |
| E | ASP188 |
| E | PHE191 |
| E | ASP218 |
| E | LYS221 |
| E | LYS229 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue EQJ F 401 |
| Chain | Residue |
| E | SER248 |
| E | ASP249 |
| E | ILE250 |
| E | HOH507 |
| F | THR12 |
| F | ASP27 |
| F | GLY28 |
| F | HIS29 |
| F | SER89 |
| F | SER90 |
| F | SER91 |
| F | PHE115 |
| F | THR156 |
| F | ASN160 |
| F | ASP188 |
| F | PHE191 |
| F | ASP218 |
| F | LYS221 |
| F | LYS229 |
| F | ARG352 |
| F | HOH526 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | binding site for residue EQJ G 401 |
| Chain | Residue |
| G | THR12 |
| G | ASP27 |
| G | GLY28 |
| G | HIS29 |
| G | SER89 |
| G | SER90 |
| G | SER91 |
| G | PHE115 |
| G | ASN117 |
| G | THR156 |
| G | ASN160 |
| G | ASP188 |
| G | PHE191 |
| G | LYS221 |
| G | LYS229 |
| G | ARG352 |
| G | HOH517 |
| H | SER248 |
| H | ASP249 |
| H | ILE250 |
| H | LEU251 |
| H | HOH506 |
| site_id | AC8 |
| Number of Residues | 20 |
| Details | binding site for residue EQJ H 401 |
| Chain | Residue |
| G | SER248 |
| G | ASP249 |
| G | ILE250 |
| H | THR12 |
| H | ASP27 |
| H | GLY28 |
| H | HIS29 |
| H | SER89 |
| H | SER90 |
| H | SER91 |
| H | PHE115 |
| H | ASN117 |
| H | THR156 |
| H | ASN160 |
| H | ASP188 |
| H | PHE191 |
| H | LYS221 |
| H | LYS229 |
| H | ARG352 |
| H | HOH510 |
