1IYE
CRYSTAL STRUCTURE OF ESCHELICHIA 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 | 26 |
| Details | BINDING SITE FOR RESIDUE PGU A 513 |
| Chain | Residue |
| A | GLY38 |
| A | ALA195 |
| A | GLY196 |
| A | GLU197 |
| A | ASN198 |
| A | LEU217 |
| A | GLY219 |
| A | ILE220 |
| A | THR221 |
| A | GLY256 |
| A | THR257 |
| A | ARG59 |
| A | ALA258 |
| A | HOH539 |
| A | HOH546 |
| A | HOH559 |
| B | TYR31 |
| B | GLY108 |
| B | VAL109 |
| A | TYR95 |
| A | ARG97 |
| A | TYR129 |
| A | ARG148 |
| A | LYS159 |
| A | TYR164 |
| A | GLU193 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE PGU B 913 |
| Chain | Residue |
| A | TYR31 |
| A | GLY108 |
| A | VAL109 |
| B | GLY38 |
| B | ARG59 |
| B | TYR95 |
| B | ARG97 |
| B | TYR129 |
| B | ARG148 |
| B | LYS159 |
| B | TYR164 |
| B | GLU193 |
| B | ALA195 |
| B | GLY196 |
| B | GLU197 |
| B | ASN198 |
| B | LEU217 |
| B | GLY219 |
| B | ILE220 |
| B | THR221 |
| B | GLY256 |
| B | THR257 |
| B | ALA258 |
| B | HOH922 |
| B | HOH927 |
| B | HOH932 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE PGU C 1413 |
| Chain | Residue |
| C | TYR31 |
| C | GLY38 |
| C | ARG59 |
| C | TYR95 |
| C | ARG97 |
| C | GLY108 |
| C | VAL109 |
| C | TYR129 |
| C | ARG148 |
| C | LYS159 |
| C | TYR164 |
| C | GLU193 |
| C | ALA195 |
| C | GLY196 |
| C | GLU197 |
| C | ASN198 |
| C | LEU217 |
| C | GLY219 |
| C | ILE220 |
| C | THR221 |
| C | GLY256 |
| C | THR257 |
| C | ALA258 |
| C | HOH1425 |
| C | HOH1430 |
| C | HOH1448 |
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 | LYS159 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1iyd |
| Chain | Residue | Details |
| C | LYS159 |
| 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 | LYS159 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 813 |
| Chain | Residue | Details |
| C | LYS159 | proton shuttle (general acid/base) |
