5DJ1
Structure of the PLP-Dependent L-Arginine Hydroxylase MppP Holoenzyme
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 | 3 |
| Details | binding site for residue CL A 500 |
| Chain | Residue |
| A | GLY28 |
| A | ASN160 |
| A | ARG352 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 500 |
| Chain | Residue |
| B | GLY28 |
| B | ASN160 |
| B | ARG352 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| D | HOH632 |
| D | HOH648 |
| D | HOH756 |
| B | ASP116 |
| B | HOH609 |
| B | HOH790 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 500 |
| Chain | Residue |
| C | GLY28 |
| C | ASN160 |
| C | ARG352 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue CL D 500 |
| Chain | Residue |
| D | GLY28 |
| D | ASN160 |
| D | LLP221 |
| D | ARG352 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | binding site for Di-peptide GLY B 220 and LLP B 221 |
| Chain | Residue |
| A | HOH625 |
| B | GLY28 |
| B | HIS29 |
| B | SER89 |
| B | SER90 |
| B | SER91 |
| B | PHE115 |
| B | THR156 |
| B | ASN160 |
| B | ASP188 |
| B | SER190 |
| B | PHE194 |
| B | ASP218 |
| B | THR219 |
| B | LEU222 |
| B | TRP223 |
| B | LYS229 |
| B | HOH608 |
| B | HOH625 |
| B | HOH628 |
| B | HOH629 |
| B | HOH649 |
| B | HOH652 |
| B | HOH689 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide LLP B 221 and LEU B 222 |
| Chain | Residue |
| A | HOH625 |
| B | GLY28 |
| B | HIS29 |
| B | SER89 |
| B | SER90 |
| B | SER91 |
| B | PHE115 |
| B | THR156 |
| B | ASN160 |
| B | ASP188 |
| B | SER190 |
| B | GLY193 |
| B | PHE194 |
| B | THR219 |
| B | GLY220 |
| B | TRP223 |
| B | LYS229 |
| B | LEU277 |
| B | HOH625 |
| B | HOH628 |
| B | HOH629 |
| B | HOH649 |
| B | HOH652 |
| B | HOH688 |
| B | HOH689 |
| site_id | AC8 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide GLY C 220 and LLP C 221 |
| Chain | Residue |
| C | GLY28 |
| C | HIS29 |
| C | SER89 |
| C | SER90 |
| C | SER91 |
| C | PHE115 |
| C | THR156 |
| C | ASN160 |
| C | ASP188 |
| C | SER190 |
| C | PHE194 |
| C | ASP218 |
| C | THR219 |
| C | LEU222 |
| C | TRP223 |
| C | LYS229 |
| C | HOH613 |
| C | HOH628 |
| C | HOH630 |
| C | HOH632 |
| C | HOH647 |
| C | HOH652 |
| C | HOH666 |
| C | HOH744 |
| D | HOH631 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide LLP C 221 and LEU C 222 |
| Chain | Residue |
| C | THR156 |
| C | ASN160 |
| C | ASP188 |
| C | SER190 |
| C | GLY193 |
| C | PHE194 |
| C | THR219 |
| C | GLY220 |
| C | TRP223 |
| C | LYS229 |
| C | LEU277 |
| C | HOH613 |
| C | HOH628 |
| C | HOH630 |
| C | HOH642 |
| C | HOH647 |
| C | HOH652 |
| C | HOH666 |
| D | HOH631 |
| C | GLY28 |
| C | HIS29 |
| C | SER89 |
| C | SER90 |
| C | SER91 |
| C | PHE115 |
| site_id | AD1 |
| Number of Residues | 26 |
| Details | binding site for Di-peptide GLY D 220 and LLP D 221 |
| Chain | Residue |
| C | HOH609 |
| D | GLY28 |
| D | HIS29 |
| D | SER89 |
| D | SER90 |
| D | SER91 |
| D | PHE115 |
| D | THR156 |
| D | ASN160 |
| D | ASP188 |
| D | SER190 |
| D | PHE191 |
| D | PHE194 |
| D | ASP218 |
| D | THR219 |
| D | LEU222 |
| D | TRP223 |
| D | LYS229 |
| D | CL500 |
| D | HOH606 |
| D | HOH610 |
| D | HOH614 |
| D | HOH618 |
| D | HOH630 |
| D | HOH642 |
| D | HOH703 |
| site_id | AD2 |
| Number of Residues | 27 |
| Details | binding site for Di-peptide LLP D 221 and LEU D 222 |
| Chain | Residue |
| C | HOH609 |
| D | GLY28 |
| D | HIS29 |
| D | SER89 |
| D | SER90 |
| D | SER91 |
| D | PHE115 |
| D | THR156 |
| D | ASN160 |
| D | ASP188 |
| D | SER190 |
| D | PHE191 |
| D | GLY193 |
| D | PHE194 |
| D | THR219 |
| D | GLY220 |
| D | TRP223 |
| D | LYS229 |
| D | LEU277 |
| D | CL500 |
| D | HOH606 |
| D | HOH614 |
| D | HOH618 |
| D | HOH630 |
| D | HOH642 |
| D | HOH695 |
| D | HOH703 |
