3UZB
Crystal Structures of Branched-Chain Aminotransferase from Deinococcus radiodurans Complexes with alpha-Ketoisocaproate and L-Glutamate Suggest Its Radio-Resistance for Catalysis
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 | 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 | 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 | 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 | 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 | 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 | 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 |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| D | 0009081 | biological_process | branched-chain amino acid metabolic process |
| D | 0009098 | biological_process | L-leucine biosynthetic process |
| D | 0009099 | biological_process | L-valine biosynthetic process |
| D | 0052654 | molecular_function | L-leucine:2-oxoglutarate transaminase activity |
| D | 0052655 | molecular_function | L-valine:2-oxoglutarate transaminase activity |
| D | 0052656 | molecular_function | L-isoleucine:2-oxoglutarate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 371 |
| Chain | Residue |
| A | ARG100 |
| A | ILE266 |
| A | THR267 |
| A | GLY303 |
| A | THR304 |
| A | COI1517 |
| A | LYS202 |
| A | TYR207 |
| A | GLU238 |
| A | GLY240 |
| A | ALA241 |
| A | ALA242 |
| A | ASN243 |
| A | SER265 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE COI A 1517 |
| Chain | Residue |
| A | PHE76 |
| A | TYR143 |
| A | LYS202 |
| A | ALA241 |
| A | THR304 |
| A | ALA305 |
| A | ALA306 |
| A | PLP371 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 372 |
| Chain | Residue |
| B | ARG100 |
| B | LYS202 |
| B | TYR207 |
| B | GLU238 |
| B | GLY240 |
| B | ALA241 |
| B | ALA242 |
| B | LEU263 |
| B | SER265 |
| B | ILE266 |
| B | THR267 |
| B | GLY303 |
| B | THR304 |
| B | COI2517 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COI B 2517 |
| Chain | Residue |
| A | VAL157 |
| B | PHE31 |
| B | TYR143 |
| B | TYR175 |
| B | LYS202 |
| B | ALA241 |
| B | THR304 |
| B | ALA305 |
| B | ALA306 |
| B | HOH367 |
| B | PLP372 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP C 373 |
| Chain | Residue |
| C | ARG100 |
| C | ARG192 |
| C | LYS202 |
| C | TYR207 |
| C | GLU238 |
| C | GLY240 |
| C | ALA241 |
| C | ALA242 |
| C | ASN243 |
| C | LEU263 |
| C | SER265 |
| C | ILE266 |
| C | THR267 |
| C | GLY303 |
| C | THR304 |
| C | COI3517 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE COI C 3517 |
| Chain | Residue |
| C | GLY78 |
| C | TYR143 |
| C | TYR175 |
| C | THR304 |
| C | ALA305 |
| C | PLP373 |
| D | VAL157 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 374 |
| Chain | Residue |
| D | ARG100 |
| D | LYS202 |
| D | TYR207 |
| D | GLU238 |
| D | ALA239 |
| D | ALA241 |
| D | ALA242 |
| D | LEU263 |
| D | SER265 |
| D | ILE266 |
| D | THR267 |
| D | GLY303 |
| D | THR304 |
| D | COI4517 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE COI D 4517 |
| Chain | Residue |
| D | PHE76 |
| D | GLY78 |
| D | TYR143 |
| D | LYS202 |
| D | TYR207 |
| D | ALA241 |
| D | THR304 |
| D | ALA305 |
| D | PLP374 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 31 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EaGaaNFFaitqdgqk....FvTpqspsi..LpSItK |
| Chain | Residue | Details |
| A | GLU238-LYS268 |
