6F77
Crystal structure of the prephenate aminotransferase from Rhizobium meliloti
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0008483 | molecular_function | transaminase activity |
| E | 0009058 | biological_process | biosynthetic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004069 | molecular_function | L-aspartate:2-oxoglutarate aminotransferase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0008483 | molecular_function | transaminase activity |
| F | 0009058 | biological_process | biosynthetic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0033854 | molecular_function | glutamate-prephenate aminotransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue PLP A 600 |
| Chain | Residue |
| A | GLY99 |
| A | TYR207 |
| A | SER239 |
| A | LYS240 |
| A | ARG248 |
| A | HOH761 |
| B | TYR64 |
| B | HOH688 |
| A | GLY100 |
| A | LYS101 |
| A | TRP125 |
| A | TYR128 |
| A | ASN171 |
| A | ASN175 |
| A | ASP204 |
| A | MET206 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue PLP C 600 |
| Chain | Residue |
| C | GLY99 |
| C | GLY100 |
| C | LYS101 |
| C | TRP125 |
| C | ASN171 |
| C | ASN175 |
| C | ASP204 |
| C | MET206 |
| C | TYR207 |
| C | SER239 |
| C | LYS240 |
| C | ARG248 |
| C | HOH743 |
| D | TYR64 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue PLP D 600 |
| Chain | Residue |
| C | TYR64 |
| D | GLY99 |
| D | GLY100 |
| D | LYS101 |
| D | TRP125 |
| D | ASN171 |
| D | ASN175 |
| D | ASP204 |
| D | MET206 |
| D | TYR207 |
| D | SER239 |
| D | LYS240 |
| D | ARG248 |
| D | HOH723 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue PLP E 600 |
| Chain | Residue |
| E | GLY99 |
| E | GLY100 |
| E | LYS101 |
| E | TRP125 |
| E | ASN171 |
| E | ASN175 |
| E | ASP204 |
| E | MET206 |
| E | TYR207 |
| E | SER239 |
| E | LYS240 |
| E | ARG248 |
| E | HOH793 |
| F | TYR64 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for Di-peptide PLP F 600 and LYS F 240 |
| Chain | Residue |
| E | TYR64 |
| E | HOH861 |
| F | GLY39 |
| F | PRO41 |
| F | GLY99 |
| F | GLY100 |
| F | LYS101 |
| F | TRP125 |
| F | ASN171 |
| F | ASN175 |
| F | ASP204 |
| F | MET206 |
| F | TYR207 |
| F | VAL238 |
| F | SER239 |
| F | ALA241 |
| F | TYR242 |
| F | ALA243 |
| F | ARG248 |
| F | HOH743 |
| F | HOH794 |
| F | HOH846 |
Functional Information from PROSITE/UniProt
| site_id | PS00105 |
| Number of Residues | 14 |
| Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. GVSKayAMtGWRIG |
| Chain | Residue | Details |
| B | GLY237-GLY250 | |
| A | GLY237-GLY250 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00509 |
| Chain | Residue | Details |
| B | GLY39 | |
| C | GLY39 | |
| D | GLY39 | |
| E | GLY39 | |
| F | GLY39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q56232 |
| Chain | Residue | Details |
| B | TRP125 | |
| E | TRP125 | |
| E | ASN175 | |
| E | ARG376 | |
| F | TRP125 | |
| F | ASN175 | |
| F | ARG376 | |
| B | ASN175 | |
| B | ARG376 | |
| C | TRP125 | |
| C | ASN175 | |
| C | ARG376 | |
| D | TRP125 | |
| D | ASN175 | |
| D | ARG376 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Important for prephenate aminotransferase activity => ECO:0000269|PubMed:30771275 |
| Chain | Residue | Details |
| B | LYS12 | |
| C | LYS12 | |
| D | LYS12 | |
| E | LYS12 | |
| F | LYS12 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:Q56232 |
| Chain | Residue | Details |
| B | LLP240 | |
| C | LYS240 | |
| D | LYS240 | |
| E | LYS240 | |
| F | LYS240 |
