Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008483 | molecular_function | transaminase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
B | 0008483 | molecular_function | transaminase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0042802 | molecular_function | identical protein binding |
C | 0008483 | molecular_function | transaminase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0042802 | molecular_function | identical protein binding |
D | 0008483 | molecular_function | transaminase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for Di-peptide PLP A 1001 and LYS A 280 |
Chain | Residue |
A | SER114 |
A | ASN253 |
A | LYS280 |
A | HOH1121 |
A | HOH1144 |
A | HOH1158 |
B | PHE308 |
B | THR309 |
A | GLY115 |
A | SER116 |
A | TYR142 |
A | HIS143 |
A | GLU217 |
A | ASP222 |
A | ASP250 |
A | VAL252 |
site_id | AC2 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP B 1001 and LYS B 280 |
Chain | Residue |
A | PHE308 |
A | THR309 |
B | ALA54 |
B | ALA56 |
B | SER114 |
B | GLY115 |
B | SER116 |
B | TYR142 |
B | HIS143 |
B | GLU217 |
B | ASP250 |
B | VAL252 |
B | ASN253 |
B | GLY279 |
B | SER281 |
B | LEU282 |
B | GLY285 |
B | HOH1122 |
B | HOH1150 |
B | HOH1158 |
B | HOH1179 |
B | HOH1281 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP C 1001 and LYS C 280 |
Chain | Residue |
C | ALA54 |
C | ALA56 |
C | SER114 |
C | GLY115 |
C | SER116 |
C | TYR142 |
C | HIS143 |
C | GLU217 |
C | ASP222 |
C | ASP250 |
C | VAL252 |
C | ASN253 |
C | GLY279 |
C | SER281 |
C | LEU282 |
C | GLY285 |
C | HOH1135 |
C | HOH1145 |
C | HOH1163 |
C | HOH1168 |
D | PHE308 |
D | THR309 |
site_id | AC4 |
Number of Residues | 23 |
Details | binding site for Di-peptide PLP D 1001 and LYS D 280 |
Chain | Residue |
C | PHE308 |
C | THR309 |
D | ALA54 |
D | ALA56 |
D | SER114 |
D | GLY115 |
D | SER116 |
D | TYR142 |
D | HIS143 |
D | GLU217 |
D | ASP222 |
D | ASP250 |
D | VAL252 |
D | ASN253 |
D | GLY279 |
D | SER281 |
D | LEU282 |
D | GLY285 |
D | HOH1108 |
D | HOH1141 |
D | HOH1143 |
D | HOH1152 |
D | HOH1186 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 39 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FAiDEVnq.GLgRtGkmwaiqqfkdiep...DLMsvGKslaSG |
Chain | Residue | Details |
A | PHE247-GLY285 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLY115 | |
C | TYR142 | |
C | ASP250 | |
C | THR309 | |
D | GLY115 | |
D | TYR142 | |
D | ASP250 | |
D | THR309 | |
A | TYR142 | |
A | ASP250 | |
A | THR309 | |
B | GLY115 | |
B | TYR142 | |
B | ASP250 | |
B | THR309 | |
C | GLY115 | |
Chain | Residue | Details |
A | LYS280 | |
B | LYS280 | |
C | LYS280 | |
D | LYS280 | |