5I5X
X-RAY CRYSTAL STRUCTURE AT 1.65A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A THIAZOLE COMPOUND AND PMP 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 | 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 | 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 PMP A 401 |
| Chain | Residue |
| A | ARG99 |
| A | GLY268 |
| A | VAL269 |
| A | VAL270 |
| A | GLY312 |
| A | THR313 |
| A | HOH532 |
| A | HOH634 |
| A | HOH643 |
| A | ARG192 |
| A | LYS202 |
| A | TYR207 |
| A | GLU237 |
| A | THR240 |
| A | MET241 |
| A | ASN242 |
| A | LEU266 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 68C A 402 |
| Chain | Residue |
| A | PHE30 |
| A | PHE75 |
| A | LYS79 |
| A | TYR141 |
| A | VAL170 |
| A | TYR173 |
| A | LYS202 |
| A | ALA314 |
| A | HOH529 |
| A | HOH541 |
| A | HOH603 |
| A | HOH648 |
| A | HOH742 |
| A | HOH831 |
| A | HOH863 |
| B | VAL155 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | LYS79 |
| A | GLN316 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 404 |
| Chain | Residue |
| A | ARG102 |
| A | HOH755 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 405 |
| Chain | Residue |
| A | ARG92 |
| A | TRP94 |
| A | HOH826 |
| A | HOH828 |
| A | HOH899 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | TYR246 |
| A | ARG306 |
| A | ARG344 |
| A | HOH606 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | GLU42 |
| A | LEU59 |
| A | THR60 |
| A | LEU162 |
| A | HOH524 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 408 |
| Chain | Residue |
| A | GLN11 |
| A | LEU12 |
| A | ASP187 |
| A | ALA189 |
| A | PHE190 |
| A | ARG220 |
| A | HOH504 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 409 |
| Chain | Residue |
| A | LEU115 |
| A | GLU116 |
| A | GLU119 |
| A | HOH507 |
| A | HOH709 |
| A | HOH753 |
| A | HOH803 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 410 |
| Chain | Residue |
| A | GLY282 |
| A | GLU283 |
| A | PHE284 |
| A | HOH928 |
| B | HOH738 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 411 |
| Chain | Residue |
| A | GLN279 |
| A | VAL286 |
| A | GLU288 |
| A | HOH598 |
| A | HOH611 |
| A | HOH640 |
| A | HOH679 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 412 |
| Chain | Residue |
| A | ARG106 |
| A | GLY196 |
| A | GLY197 |
| A | HOH704 |
| B | PHE190 |
| B | ILE191 |
| B | PRO209 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 413 |
| Chain | Residue |
| A | HIS249 |
| A | GLN295 |
| B | ASP85 |
| B | ARG89 |
| B | GLY355 |
| B | ILE356 |
| B | HOH594 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 414 |
| Chain | Residue |
| A | ASP276 |
| A | MET277 |
| A | THR280 |
| A | GLU348 |
| A | ARG357 |
| A | HIS359 |
| A | HOH501 |
| A | HOH513 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 415 |
| Chain | Residue |
| A | TRP94 |
| A | HOH515 |
| A | HOH788 |
| site_id | AD7 |
| Number of Residues | 16 |
| Details | binding site for residue PMP B 401 |
| Chain | Residue |
| B | ARG99 |
| B | ARG192 |
| B | LYS202 |
| B | TYR207 |
| B | GLU237 |
| B | THR240 |
| B | ASN242 |
| B | LEU266 |
| B | GLY268 |
| B | VAL269 |
| B | VAL270 |
| B | GLY312 |
| B | THR313 |
| B | HOH523 |
| B | HOH648 |
| B | HOH693 |
| site_id | AD8 |
| Number of Residues | 15 |
| Details | binding site for residue 68C B 402 |
| Chain | Residue |
| A | VAL155 |
| B | PHE30 |
| B | PHE75 |
| B | LYS79 |
| B | TYR141 |
| B | TYR173 |
| B | LYS202 |
| B | ALA314 |
| B | HOH536 |
| B | HOH615 |
| B | HOH643 |
| B | HOH682 |
| B | HOH717 |
| B | HOH823 |
| B | HOH901 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | LYS79 |
| B | GLN316 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 404 |
| Chain | Residue |
| B | HOH806 |
| B | HOH885 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 405 |
| Chain | Residue |
| B | ARG92 |
| B | TRP94 |
| B | HOH533 |
| B | HOH759 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 406 |
| Chain | Residue |
| B | TYR246 |
| B | ARG306 |
| B | GLU340 |
| B | ARG344 |
| B | HOH517 |
| B | HOH527 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 407 |
| Chain | Residue |
| B | GLU42 |
| B | ARG52 |
| B | LEU59 |
| B | THR60 |
| B | LEU162 |
| B | HOH550 |
| B | HOH722 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 408 |
| Chain | Residue |
| B | GLY282 |
| B | PHE284 |
| B | HOH567 |
| B | HOH746 |
| site_id | AE6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 409 |
| Chain | Residue |
| B | LEU300 |
| B | GLU301 |
| B | ASN329 |
| B | LEU330 |
| B | HIS331 |
| B | HOH638 |
| B | HOH860 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 410 |
| Chain | Residue |
| B | TRP94 |
| B | HOH521 |
| B | HOH533 |
| B | HOH618 |
| site_id | AE8 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 411 |
| Chain | Residue |
| B | ASP276 |
| B | MET277 |
| B | THR280 |
| B | GLU348 |
| B | HIS359 |
| B | HOH512 |
| B | HOH591 |
| B | HOH728 |
| B | HOH798 |
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 |
