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 | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004084 | molecular_function | branched-chain-amino-acid transaminase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| 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 | 0016740 | molecular_function | transferase activity |
| 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 |
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 site: {"evidences":[{"source":"PubMed","id":"12269802","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16141215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17050531","evidenceCode":"ECO:0000269"}]} |
| 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 |
