5BWX
X-RAY CRYSTAL STRUCTURE AT 1.70A RESOLUTION OF HUMAN MITOCHONDRIAL BRANCHED CHAIN AMINOTRANSFERASE (BCATM) COMPLEXED WITH A 4-CHLORO-2-FLUORO SUBSTITUTED PYRAZOLOPYRIMIDINONE 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 | 4W4402 |
A | HOH568 |
A | HOH669 |
A | HOH693 |
A | ARG192 |
A | LYS202 |
A | TYR207 |
A | GLU237 |
A | THR240 |
A | ASN242 |
A | LEU266 |
A | GLY268 |
site_id | AC2 |
Number of Residues | 19 |
Details | binding site for residue 4W4 A 402 |
Chain | Residue |
A | TYR141 |
A | ARG143 |
A | VAL182 |
A | LYS202 |
A | GLN224 |
A | VAL238 |
A | GLY239 |
A | THR240 |
A | MET241 |
A | GLY312 |
A | ALA314 |
A | CYS315 |
A | CYS318 |
A | PLP401 |
A | EDO403 |
A | HOH630 |
A | HOH674 |
B | LEU153 |
B | VAL155 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue EDO A 403 |
Chain | Residue |
A | CYS315 |
A | 4W4402 |
A | HOH668 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 404 |
Chain | Residue |
A | ASP276 |
A | THR280 |
A | GLU348 |
A | ARG357 |
A | HIS359 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | ARG102 |
A | PRO267 |
A | HOH652 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | TYR246 |
A | ARG306 |
A | ARG344 |
A | HOH575 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 407 |
Chain | Residue |
A | GLU42 |
A | LEU59 |
A | THR60 |
A | HOH594 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue EDO A 408 |
Chain | Residue |
A | GLN234 |
A | ASN262 |
A | THR290 |
A | HOH663 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO A 409 |
Chain | Residue |
A | TRP94 |
A | HOH736 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue EDO A 410 |
Chain | Residue |
A | ARG106 |
A | GLY196 |
A | GLY197 |
A | HOH619 |
B | ILE191 |
B | PRO209 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue EDO A 411 |
Chain | Residue |
A | GLN16 |
A | TRP194 |
A | TYR229 |
A | GLY230 |
A | HOH512 |
A | HOH534 |
A | HOH617 |
B | TRP194 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 412 |
Chain | Residue |
A | GLU216 |
A | HOH692 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 413 |
Chain | Residue |
A | TRP94 |
A | ASP98 |
A | LYS114 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 414 |
Chain | Residue |
A | ARG102 |
A | ASN200 |
A | TYR201 |
A | CL416 |
A | HOH604 |
A | HOH694 |
A | HOH717 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue EDO A 415 |
Chain | Residue |
A | ASN200 |
A | LEU261 |
A | ASN262 |
A | HOH513 |
A | HOH717 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue CL A 416 |
Chain | Residue |
A | EDO414 |
A | HOH513 |
site_id | AD8 |
Number of Residues | 4 |
Details | binding site for residue GOL A 417 |
Chain | Residue |
A | PRO260 |
A | LEU261 |
A | HOH520 |
A | HOH660 |
site_id | AD9 |
Number of Residues | 18 |
Details | binding site for residue 4W4 B 402 |
Chain | Residue |
B | TYR141 |
B | ARG143 |
B | VAL182 |
B | LYS202 |
B | GLN224 |
B | VAL238 |
B | GLY239 |
B | THR240 |
B | MET241 |
B | GLY312 |
B | ALA314 |
B | CYS315 |
B | CYS318 |
B | PLP401 |
B | EDO404 |
B | HOH640 |
B | HOH681 |
A | VAL155 |
site_id | AE1 |
Number of Residues | 5 |
Details | binding site for residue DMS B 403 |
Chain | Residue |
B | MET40 |
B | GLU42 |
B | LEU59 |
B | THR60 |
B | HOH595 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 404 |
Chain | Residue |
B | PHE30 |
B | TYR173 |
B | 4W4402 |
B | HOH766 |
site_id | AE3 |
Number of Residues | 6 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | ASP276 |
B | THR280 |
B | GLU348 |
B | HIS359 |
B | TRP361 |
B | HOH520 |
site_id | AE4 |
Number of Residues | 5 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | TYR246 |
B | ARG306 |
B | GLU340 |
B | ARG344 |
B | HOH652 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | GLU336 |
B | ASN337 |
B | HOH551 |
B | HOH592 |
site_id | AE6 |
Number of Residues | 3 |
Details | binding site for residue GOL B 409 |
Chain | Residue |
B | HOH539 |
B | HOH674 |
B | HOH718 |
site_id | AE7 |
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 | 4W4402 |
B | HOH575 |
B | HOH588 |
B | HOH659 |
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 |