5I5Y
X-RAY CRYSTAL STRUCTURE AT 1.81A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH AN ARYL ACETATE 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 | L-valine biosynthetic process |
A | 0010817 | biological_process | regulation of hormone levels |
A | 0050048 | molecular_function | obsolete L-leucine:2-oxoglutarate aminotransferase activity |
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 |
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 | L-valine biosynthetic process |
B | 0010817 | biological_process | regulation of hormone levels |
B | 0050048 | molecular_function | obsolete L-leucine:2-oxoglutarate aminotransferase activity |
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 |
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 | 68D402 |
A | HOH567 |
A | HOH580 |
A | HOH685 |
A | ARG192 |
A | LYS202 |
A | TYR207 |
A | GLU237 |
A | THR240 |
A | ASN242 |
A | LEU266 |
A | GLY268 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue 68D A 402 |
Chain | Residue |
A | PHE30 |
A | LYS79 |
A | TYR141 |
A | VAL170 |
A | TYR173 |
A | LYS202 |
A | THR240 |
A | GLY312 |
A | THR313 |
A | ALA314 |
A | PLP401 |
A | EDO404 |
A | HOH511 |
A | HOH514 |
A | HOH556 |
A | HOH572 |
A | HOH589 |
A | HOH712 |
B | TYR70 |
B | VAL155 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue CL A 403 |
Chain | Residue |
A | HOH783 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | LEU28 |
A | PHE30 |
A | ALA172 |
A | TYR173 |
A | 68D402 |
A | HOH502 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | TYR246 |
A | ARG306 |
A | GLU340 |
A | ARG344 |
A | HOH541 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | MET40 |
A | GLU42 |
A | ARG52 |
A | LEU59 |
A | THR60 |
A | LEU162 |
A | HOH676 |
site_id | AC7 |
Number of Residues | 21 |
Details | binding site for residue 68D B 402 |
Chain | Residue |
A | TYR70 |
A | VAL155 |
B | PHE30 |
B | LYS79 |
B | TYR141 |
B | VAL170 |
B | TYR173 |
B | LYS202 |
B | TYR207 |
B | THR240 |
B | GLY312 |
B | THR313 |
B | ALA314 |
B | PLP401 |
B | HOH508 |
B | HOH532 |
B | HOH561 |
B | HOH574 |
B | HOH647 |
B | HOH714 |
B | HOH754 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL B 403 |
Chain | Residue |
B | LYS79 |
B | GLN316 |
B | HOH699 |
B | HOH768 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue CL B 404 |
Chain | Residue |
B | HOH851 |
B | HOH964 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CL B 405 |
Chain | Residue |
B | ARG92 |
B | TRP94 |
B | HOH620 |
B | HOH807 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | LEU115 |
B | GLU116 |
B | GLU119 |
B | HOH528 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | TRP94 |
B | ASP98 |
B | LYS114 |
B | HOH770 |
site_id | AD4 |
Number of Residues | 6 |
Details | binding site for residue EDO B 408 |
Chain | Residue |
B | LEU162 |
B | HOH746 |
B | MET40 |
B | ARG52 |
B | LEU59 |
B | THR60 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 409 |
Chain | Residue |
B | ASP85 |
B | TYR354 |
B | GLY355 |
B | ILE356 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO B 410 |
Chain | Residue |
B | TYR246 |
B | GLU340 |
B | ARG344 |
B | HOH579 |
B | HOH786 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue EDO B 411 |
Chain | Residue |
B | ARG99 |
B | ARG102 |
B | PRO267 |
B | HOH678 |
B | HOH745 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue GOL B 412 |
Chain | Residue |
B | HOH620 |
B | HOH661 |
B | HOH770 |
B | HOH807 |
site_id | AD9 |
Number of Residues | 21 |
Details | binding site for Di-peptide PLP B 401 and LYS B 202 |
Chain | Residue |
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 |
B | THR313 |
B | 68D402 |
B | HOH516 |
B | HOH640 |
B | HOH685 |
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 |