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 | 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 |
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 |