5DJ3
Structure of the PLP-Dependent L-Arginine Hydroxylase MppP with D-Arginine Bound
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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue 5DK A 500 |
| Chain | Residue |
| A | ASP27 |
| A | ASP188 |
| A | SER190 |
| A | PHE191 |
| A | LYS221 |
| A | ASP227 |
| A | LYS229 |
| A | ARG352 |
| A | HOH601 |
| A | HOH605 |
| A | HOH615 |
| A | GLY28 |
| A | HOH736 |
| C | LEU252 |
| A | HIS29 |
| A | SER89 |
| A | SER90 |
| A | SER91 |
| A | PHE115 |
| A | THR156 |
| A | ASN160 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue 5DK B 401 |
| Chain | Residue |
| B | ASP27 |
| B | GLY28 |
| B | HIS29 |
| B | SER89 |
| B | SER90 |
| B | SER91 |
| B | PHE115 |
| B | THR156 |
| B | ASN160 |
| B | ASP188 |
| B | SER190 |
| B | PHE191 |
| B | LYS221 |
| B | ASP227 |
| B | LYS229 |
| B | ARG352 |
| B | HOH503 |
| B | HOH518 |
| B | HOH519 |
| D | LEU252 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ASP116 |
| B | ASP120 |
| B | HOH521 |
| B | HOH532 |
| B | HOH653 |
| C | HOH702 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue 5DK C 500 |
| Chain | Residue |
| A | HOH640 |
| C | ASP27 |
| C | GLY28 |
| C | HIS29 |
| C | SER89 |
| C | SER90 |
| C | SER91 |
| C | PHE115 |
| C | THR156 |
| C | ASN160 |
| C | ASP188 |
| C | PHE191 |
| C | LYS221 |
| C | ASP227 |
| C | LYS229 |
| C | ARG352 |
| C | HOH604 |
| C | HOH618 |
| C | HOH636 |
| C | HOH668 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | binding site for residue 5DK D 500 |
| Chain | Residue |
| B | LEU252 |
| D | ASP27 |
| D | GLY28 |
| D | HIS29 |
| D | SER89 |
| D | SER90 |
| D | SER91 |
| D | PHE115 |
| D | THR156 |
| D | ASN160 |
| D | ASP188 |
| D | PHE191 |
| D | LYS221 |
| D | ASP227 |
| D | LYS229 |
| D | ARG352 |
| D | HOH628 |
| D | HOH630 |
| D | HOH635 |






