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 |