6J2V
GABA aminotransferase from Corynebacterium glutamicum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008483 | molecular_function | transaminase activity |
A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
C | 0016740 | molecular_function | transferase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
D | 0016740 | molecular_function | transferase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue PLZ A 501 |
Chain | Residue |
A | SER129 |
A | ILE261 |
A | GLN262 |
A | LYS288 |
A | HOH620 |
A | HOH657 |
A | HOH672 |
A | HOH737 |
A | HOH744 |
B | MET98 |
B | GLY316 |
A | GLY130 |
B | THR317 |
B | HOH634 |
A | ALA131 |
A | TYR157 |
A | HIS158 |
A | ARG160 |
A | GLU226 |
A | GLU231 |
A | ASP259 |
site_id | AC2 |
Number of Residues | 9 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | PHE97 |
A | MET98 |
A | TYR105 |
A | LEU126 |
A | GLY315 |
A | GLY316 |
A | GLY319 |
A | HOH709 |
B | LEU38 |
site_id | AC3 |
Number of Residues | 7 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | PRO309 |
A | GLY310 |
A | ALA313 |
A | HOH735 |
B | SER176 |
B | GLY177 |
B | HOH764 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
A | SER176 |
A | GLY177 |
A | HOH628 |
A | HOH685 |
B | ALA308 |
B | PRO309 |
B | GLY310 |
B | ALA313 |
B | HOH618 |
B | HOH757 |
site_id | AC5 |
Number of Residues | 20 |
Details | binding site for residue PLZ B 502 |
Chain | Residue |
A | GLY316 |
A | THR317 |
A | HOH640 |
B | ILE69 |
B | GLY130 |
B | ALA131 |
B | TYR157 |
B | HIS158 |
B | ARG160 |
B | GLU226 |
B | ASP259 |
B | ILE261 |
B | GLN262 |
B | LYS288 |
B | HOH651 |
B | HOH656 |
B | HOH657 |
B | HOH692 |
B | HOH732 |
B | HOH792 |
site_id | AC6 |
Number of Residues | 10 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
A | LEU38 |
B | PHE97 |
B | MET98 |
B | TYR105 |
B | LEU126 |
B | GLY315 |
B | GLY316 |
B | GLY319 |
B | HOH730 |
B | HOH835 |
site_id | AC7 |
Number of Residues | 22 |
Details | binding site for residue PLZ C 501 |
Chain | Residue |
C | ILE69 |
C | GLY130 |
C | ALA131 |
C | TYR157 |
C | HIS158 |
C | ARG160 |
C | GLU226 |
C | GLU231 |
C | ASP259 |
C | ILE261 |
C | GLN262 |
C | LYS288 |
C | HOH611 |
C | HOH627 |
C | HOH672 |
C | HOH676 |
C | HOH775 |
C | HOH779 |
D | MET98 |
D | GLY316 |
D | THR317 |
D | HOH668 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue GOL C 502 |
Chain | Residue |
C | PHE97 |
C | MET98 |
C | TYR105 |
C | LEU126 |
C | GLY315 |
C | GLY316 |
C | GLY319 |
C | HOH706 |
D | LEU38 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue GOL C 503 |
Chain | Residue |
C | PRO309 |
C | GLY310 |
C | ALA313 |
C | HOH610 |
C | HOH636 |
C | HOH831 |
D | SER176 |
D | HOH629 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue GOL D 501 |
Chain | Residue |
C | SER176 |
C | GLY177 |
C | HOH723 |
C | HOH822 |
D | PRO309 |
D | GLY310 |
D | ALA313 |
D | HOH609 |
D | HOH666 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue PLZ D 502 |
Chain | Residue |
C | MET98 |
C | GLY316 |
C | THR317 |
C | HOH665 |
D | ILE69 |
D | GLY130 |
D | ALA131 |
D | TYR157 |
D | HIS158 |
D | ARG160 |
D | GLU226 |
D | GLU231 |
D | ASP259 |
D | ILE261 |
D | GLN262 |
D | LYS288 |
D | HOH617 |
D | HOH618 |
D | HOH685 |
D | HOH687 |
D | HOH731 |
D | HOH734 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue GOL D 503 |
Chain | Residue |
C | LEU38 |
D | PHE97 |
D | MET98 |
D | TYR105 |
D | LEU126 |
D | GLY315 |
D | GLY316 |
D | GLY319 |
D | HOH670 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEIqs.GFlRtGdwfasdaegvip....DVIttAKgiaGG |
Chain | Residue | Details |
A | PHE256-GLY293 |