5I5U
X-RAY CRYSTAL STRUCTURE AT 2.40A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A TETRAHYDRONAPHTHALENYL COMPOUND AND AN INTERNAL ALDIMINE LINKED PLP COFACTOR.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006549 | biological_process | isoleucine metabolic process |
| A | 0006550 | biological_process | isoleucine catabolic process |
| A | 0006551 | biological_process | L-leucine metabolic process |
| A | 0006573 | biological_process | valine metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009081 | biological_process | branched-chain amino acid metabolic process |
| A | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| A | 0009083 | biological_process | branched-chain amino acid catabolic process |
| A | 0009098 | biological_process | L-leucine biosynthetic process |
| A | 0009099 | biological_process | valine biosynthetic process |
| A | 0010817 | biological_process | regulation of hormone levels |
| A | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
| A | 0052654 | molecular_function | L-leucine transaminase activity |
| A | 0052655 | molecular_function | L-valine transaminase activity |
| A | 0052656 | molecular_function | L-isoleucine transaminase activity |
| A | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006549 | biological_process | isoleucine metabolic process |
| B | 0006550 | biological_process | isoleucine catabolic process |
| B | 0006551 | biological_process | L-leucine metabolic process |
| B | 0006573 | biological_process | valine metabolic process |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009081 | biological_process | branched-chain amino acid metabolic process |
| B | 0009082 | biological_process | branched-chain amino acid biosynthetic process |
| B | 0009083 | biological_process | branched-chain amino acid catabolic process |
| B | 0009098 | biological_process | L-leucine biosynthetic process |
| B | 0009099 | biological_process | valine biosynthetic process |
| B | 0010817 | biological_process | regulation of hormone levels |
| B | 0050048 | molecular_function | L-leucine:2-oxoglutarate aminotransferase activity |
| B | 0052654 | molecular_function | L-leucine transaminase activity |
| B | 0052655 | molecular_function | L-valine transaminase activity |
| B | 0052656 | molecular_function | L-isoleucine transaminase activity |
| B | 1990830 | biological_process | cellular response to leukemia inhibitory factor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue PLP A 401 |
| Chain | Residue |
| A | ARG99 |
| A | VAL269 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | 67Y402 |
| A | HOH519 |
| A | HOH551 |
| A | HOH558 |
| A | ARG192 |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | ASN242 |
| A | LEU266 |
| A | GLY268 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue 67Y A 402 |
| Chain | Residue |
| A | PHE30 |
| A | PHE75 |
| A | TYR173 |
| A | LYS202 |
| A | TYR207 |
| A | THR240 |
| A | MET241 |
| A | GLY312 |
| A | THR313 |
| A | ALA314 |
| A | CYS315 |
| A | PLP401 |
| A | HOH559 |
| A | HOH666 |
| B | TYR70 |
| B | LEU153 |
| B | VAL155 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | TYR246 |
| A | LEU341 |
| A | ARG344 |
| A | HOH504 |
| A | HOH536 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | VAL195 |
| A | TYR229 |
| A | HOH646 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ASN200 |
| A | LEU261 |
| A | ASN262 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | GLU250 |
| A | ARG298 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue 67Y B 402 |
| Chain | Residue |
| A | TYR70 |
| A | LEU153 |
| A | VAL155 |
| B | PHE30 |
| B | PHE75 |
| B | TYR173 |
| B | LYS202 |
| B | TYR207 |
| B | THR240 |
| B | MET241 |
| B | GLY312 |
| B | THR313 |
| B | ALA314 |
| B | CYS315 |
| B | PLP401 |
| B | HOH514 |
| B | HOH542 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 404 |
| Chain | Residue |
| B | GLY282 |
| B | HOH623 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | ASP276 |
| B | MET277 |
| B | THR280 |
| B | GLU348 |
| B | HIS359 |
| B | HOH504 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | TYR246 |
| B | PHE284 |
| B | GLU340 |
| B | ARG344 |
| B | HOH563 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | GLU42 |
| B | LEU59 |
| B | THR60 |
| B | LEU162 |
| B | HOH639 |
| B | HOH640 |
| site_id | AD3 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide PLP B 401 and LYS B 202 |
| Chain | Residue |
| B | THR313 |
| B | 67Y402 |
| B | HOH515 |
| B | HOH524 |
| B | HOH578 |
| B | LEU74 |
| B | PHE75 |
| B | ARG99 |
| B | SER103 |
| B | ARG192 |
| B | TYR201 |
| B | LEU203 |
| B | TYR207 |
| B | GLU237 |
| B | THR240 |
| B | ASN242 |
| B | LEU266 |
| B | GLY268 |
| B | VAL269 |
| B | VAL270 |
| B | GLY312 |
Functional Information from PROSITE/UniProt
| site_id | PS00770 |
| Number of Residues | 35 |
| Details | AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EvGtmNIFvywthedgvle.LvTpplngvi.LpGVvR |
| Chain | Residue | Details |
| A | GLU237-ARG271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12269802, ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531 |
| Chain | Residue | Details |
| A | TYR141 | |
| B | TYR141 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:16141215, ECO:0000269|PubMed:17050531, ECO:0007744|PDB:2A1H, ECO:0007744|PDB:2HDK, ECO:0007744|PDB:2HG8, ECO:0007744|PDB:2HGW, ECO:0007744|PDB:2HGX, ECO:0007744|PDB:2HHF |
| Chain | Residue | Details |
| A | LYS202 | |
| B | LYS202 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS294 | |
| B | LYS294 |
