4CVQ
CRYSTAL STRUCTURE OF AN AMINOTRANSFERASE FROM ESCHERICHIA COLI AT 2. 11 ANGSTROEM RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004021 | molecular_function | L-alanine:2-oxoglutarate aminotransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006523 | biological_process | alanine biosynthetic process |
| A | 0006974 | biological_process | DNA damage response |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0019272 | biological_process | L-alanine biosynthetic process from pyruvate |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030632 | biological_process | D-alanine biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046677 | biological_process | response to antibiotic |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004021 | molecular_function | L-alanine:2-oxoglutarate aminotransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006523 | biological_process | alanine biosynthetic process |
| B | 0006974 | biological_process | DNA damage response |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0019272 | biological_process | L-alanine biosynthetic process from pyruvate |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030632 | biological_process | D-alanine biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046677 | biological_process | response to antibiotic |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 1240 |
| Chain | Residue |
| A | GLY103 |
| A | LYS240 |
| A | ARG248 |
| A | ACT1405 |
| A | HOH2044 |
| B | TYR68 |
| A | VAL104 |
| A | SER105 |
| A | TYR129 |
| A | ASN179 |
| A | ASP207 |
| A | ILE209 |
| A | TYR210 |
| A | SER239 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1240 |
| Chain | Residue |
| A | TYR68 |
| B | GLY103 |
| B | VAL104 |
| B | SER105 |
| B | TYR129 |
| B | ASN179 |
| B | ASP207 |
| B | ILE209 |
| B | TYR210 |
| B | SER239 |
| B | LYS240 |
| B | ARG248 |
| B | ACT1406 |
| B | HOH2070 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 1405 |
| Chain | Residue |
| A | ILE40 |
| A | GLY41 |
| A | TYR129 |
| A | ASN179 |
| A | TYR333 |
| A | ARG378 |
| A | PLP1240 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 1406 |
| Chain | Residue |
| B | ILE17 |
| B | ILE40 |
| B | GLY41 |
| B | TYR129 |
| B | ASN179 |
| B | TYR333 |
| B | ARG378 |
| B | PLP1240 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1407 |
| Chain | Residue |
| A | ILE4 |
| B | ASN201 |
| B | LEU202 |
| B | LEU231 |
| B | HIS260 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:25014014, ECO:0007744|PDB:4CVQ |
| Chain | Residue | Details |
| A | GLY41 | |
| A | ASN179 | |
| A | ARG378 | |
| B | GLY41 | |
| B | ASN179 | |
| B | ARG378 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:25014014, ECO:0007744|PDB:4CVQ |
| Chain | Residue | Details |
| A | LYS240 | |
| B | LYS240 |
