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 | 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 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 |