4E3R
PLP-bound aminotransferase mutant crystal structure from Vibrio fluvialis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009102 | biological_process | biotin biosynthetic process |
| C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0004015 | molecular_function | adenosylmethionine-8-amino-7-oxononanoate transaminase activity |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009102 | biological_process | biotin biosynthetic process |
| D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | PRO4 |
| B | HOH719 |
| A | GLN5 |
| A | SER6 |
| A | ALA9 |
| B | GLN5 |
| B | SER6 |
| B | ALA9 |
| B | SO4501 |
| B | HOH663 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 502 |
| Chain | Residue |
| A | VAL101 |
| A | GLU102 |
| A | SER104 |
| A | PHE106 |
| A | HOH718 |
| A | HOH735 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| A | ALA9 |
| A | SO4501 |
| A | HOH846 |
| B | PRO4 |
| B | GLN5 |
| B | ALA9 |
| B | THR13 |
| B | HOH663 |
| B | HOH803 |
| B | HOH897 |
| B | HOH922 |
| B | HOH941 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 502 |
| Chain | Residue |
| B | VAL101 |
| B | GLU102 |
| B | SER104 |
| B | PHE106 |
| B | HOH689 |
| B | HOH697 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 501 |
| Chain | Residue |
| C | VAL101 |
| C | GLU102 |
| C | SER104 |
| C | PHE106 |
| C | HOH801 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| C | PRO4 |
| C | GLN5 |
| C | SER6 |
| C | ALA9 |
| C | HOH601 |
| C | HOH909 |
| D | GLN5 |
| D | SER6 |
| D | ALA9 |
| D | HOH690 |
| D | HOH849 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 502 |
| Chain | Residue |
| D | VAL101 |
| D | GLU102 |
| D | SER104 |
| D | PHE106 |
| D | HOH652 |
| D | HOH669 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VIsDEVvc.GFgRtGntwgcvtydftp....DAIisSKnltAG |
| Chain | Residue | Details |
| A | VAL253-GLY290 |
