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:2-oxoglutarate transaminase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006550 | biological_process | L-isoleucine catabolic process |
| A | 0006574 | biological_process | L-valine catabolic 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 | 0050873 | biological_process | brown fat cell differentiation |
| 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 | 0097009 | biological_process | energy homeostasis |
| A | 1903444 | biological_process | negative regulation of brown fat cell differentiation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid:2-oxoglutarate transaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006550 | biological_process | L-isoleucine catabolic process |
| B | 0006574 | biological_process | L-valine catabolic 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 | 0050873 | biological_process | brown fat cell differentiation |
| 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 | 0097009 | biological_process | energy homeostasis |
| B | 1903444 | biological_process | negative regulation of brown fat cell differentiation |
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 | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12269802","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2A1H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HDK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HG8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HGX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HHF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
