1I1M
CRYSTAL STRUCTURE OF ESCHERICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006532 | biological_process | L-aspartate biosynthetic process |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009099 | biological_process | L-valine biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046394 | biological_process | carboxylic acid biosynthetic process |
| A | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| A | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| A | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006532 | biological_process | L-aspartate biosynthetic process |
| B | 0009081 | biological_process | branched-chain amino acid metabolic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0009099 | biological_process | L-valine biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| B | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| B | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006532 | biological_process | L-aspartate biosynthetic process |
| C | 0009081 | biological_process | branched-chain amino acid metabolic process |
| C | 0009098 | biological_process | L-leucine biosynthetic process |
| C | 0009099 | biological_process | L-valine biosynthetic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046394 | biological_process | carboxylic acid biosynthetic process |
| C | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| C | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| C | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 413 |
| Chain | Residue |
| A | ARG59 |
| A | THR221 |
| A | GLY256 |
| A | THR257 |
| A | 4MV414 |
| A | HOH417 |
| A | HOH422 |
| A | LYS159 |
| A | TYR164 |
| A | GLU193 |
| A | GLY196 |
| A | GLU197 |
| A | LEU217 |
| A | GLY219 |
| A | ILE220 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 4MV A 414 |
| Chain | Residue |
| A | GLY38 |
| A | TYR95 |
| A | LYS159 |
| A | TYR164 |
| A | GLY196 |
| A | THR257 |
| A | ALA258 |
| A | PLP413 |
| A | HOH434 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP B 913 |
| Chain | Residue |
| B | HOH36 |
| B | HOH46 |
| B | HOH101 |
| B | ARG559 |
| B | LYS659 |
| B | TYR664 |
| B | GLU693 |
| B | GLY696 |
| B | GLU697 |
| B | LEU717 |
| B | GLY719 |
| B | ILE720 |
| B | THR721 |
| B | GLY756 |
| B | THR757 |
| B | 4MV914 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 4MV B 914 |
| Chain | Residue |
| B | HOH127 |
| B | TYR595 |
| B | TYR664 |
| B | THR757 |
| B | ALA758 |
| B | PLP913 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP C 1413 |
| Chain | Residue |
| C | HOH2 |
| C | HOH25 |
| C | ARG1059 |
| C | LYS1159 |
| C | TYR1164 |
| C | GLU1193 |
| C | GLY1196 |
| C | GLU1197 |
| C | LEU1217 |
| C | GLY1219 |
| C | ILE1220 |
| C | THR1221 |
| C | GLY1256 |
| C | THR1257 |
| C | 4MV1414 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 4MV C 1414 |
| Chain | Residue |
| C | HOH117 |
| C | TYR1095 |
| C | LYS1159 |
| C | GLY1196 |
| C | THR1257 |
| C | ALA1258 |
| C | PLP1413 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 30 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgAgeNLFevkdgv......LfTppftssa.LpGItR |
| Chain | Residue | Details |
| A | GLU193-ARG222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| A | LYS159 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| B | LYS659 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| C | LYS1159 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 813 |
| Chain | Residue | Details |
| A | LYS159 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 813 |
| Chain | Residue | Details |
| B | LYS659 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 813 |
| Chain | Residue | Details |
| C | LYS1159 | proton shuttle (general acid/base) |
